Summer Intern Report Lambert P FINAL.pdf

Faculty of Pharmacy, Marwadi University | AY 2024-25 I
Practice School Training Report
Practice School Training Report
PRACTICE SCHOOL
TRAINING REPORT
Pharmacy Training at AB LAB IIT ROPARn
Submitted by
Mr. LAMBERT PHILIPO BARUGAHALE
Enrolment No.: 92101263050
Supervised by
Dr. NASIRBHAI VADIYA
ASSOCIATE PROFESSOR
FACULTY OF PHARMACY, MARWADI UNIVERSITY
A REPORT SUBMITTED TO
Faculty of Pharmacy, Marwadi University
IN PARTIAL FULFILMENT OF THE REQUIREMENTS FOR
B. Pharmacy, Semester-7
DECEMBER 2024
FACULTY OF PHARMACY, MARWADI UNIVERSITY,
RAJKOT-MORBI HIGHWAY, RAJKOT, 360003, GUJARAT, INDIA.

Faculty of Pharmacy, Marwadi University | AY 2024-25 II
CERTIFICATE
This is to certify that Mr. LAMBERT PHILIPO BARUGAHALE
(Enrolment no.: 92101263050) studying in B. Pharm. Semester 7 at the
Faculty of Pharmacy, Marwadi University has undergone 150 hours of
Practice School training at …AB LAB IIT ROPAR under my supervision
and it is up to my satisfaction.
Date: 15/07/2024
Place: IIT ROPAR, INDIA
|
Signature and Name of supervisor Signature and Name of Principal
DR. NASIRBHAI VADIA DR. LALJI BALDANIA
M. Pharm.PhD, Nasirbhai Vadia M. Pharm., PhD
Associate Professor Professor and Principle
Faculty of Pharmacy Faculty of Pharmacy
Marwadi University Marwadi University

Faculty of Pharmacy, Marwadi University | AY 2024-25 1
PEPTIDE SYNTHESIS FOR THERAPEUTIC PURPOSES AND HPLC PURIFICATION
Summer Intern Report
by
“LAMBERT PHILIPO BARUGAHALE”
(MARWADI UNIVERSITY)
(Under )
DEPARTMENT OF CHEMISTRY
INDIAN INSTITUTE OF TECHNOLOGY ROPAR July, 2024
(IIT ROPAR)

Acknowledgments
I want to express my sincere gratitude to the Indian Institute of Technology Ropar for giving me the chance
to work as an intern at the prestigious AB Lab for two months during the summer. I owe a debt of gratitude
to Dr. Anupam Bandyopadhyay for his great advice and assistance during my stay in the peptide lab. His
knowledge and guidance have greatly enhanced my educational experience.
Additionally, I want to sincerely thank my lab partners for their unwavering encouragement and wisdom.
Special thanks go out to Mr. Vinod Gaur, Mr. Bibhekananda Pati, Mr. Arnaub Chowdhury, Mr. Saurav
Chaterjee, Mr. Soumit Douta, Mr. Nitesh, Ms. Sagnika Ghosh, and Ms. Neelam Verma for their support,
encouragement, and for fostering a cooperative and supportive environment. Their help and friendship have
made my internship a fulfilling experience.
I appreciate all of your hard work, patience, and expertise that you have shared with me.

TRAINING CERTIFICATE

Table of Contents
1. Introduction
1.1 Background
1.1.1 Historical Perspective
2. Literature Review/ Theoretical Framework
3. Research Design / Methodology
4. Results and Discussion
5. Summary / Conclusions
References/Bibliography

List of Figures
Figure
Figure 1,1 Systematic diagram of the process followed in the study……….…………….…...
10
Figure 1,2: Chemical structure of Rink amide 11
Figure 1.3: Fluorenyl methoxycarbonyl protecting group 13
Figure 1.4: Tert- butyloxycarbonyl a side chain protecting group 15
Figure 1.5: The schematic presentation of major steps of the experiment
15
Figure 1.6: A chemical structure of the peptide sample CKSTLQA 18
Figure 1.7: LC-MS chromatogram data 18
Figure 1.8: Chemical structure of peptide sample CVVSSRHT
Figure 1.9 : LC-MS chromatogram data 21
Figure 2.1.: Mass LC-MS data of sample CVVSSRHT 22
Figure 2.2: A chemical structural representation of peptide sample KAKAK 25
Figure 2.3: A recorded peak of the sample LPB-X-24 25
Figure 2.4: A recorded mass data of sample LPB-X-24 28
Figure 2.5: A chemical structure of the sample RRDYQMRRKARAGY 28
Figure 2.6: A recorded mass data of the sample 29
Figure 2.7: A recorded data of the peptide 29
Figure 2.8: Prescription VI 31
Figure 2.9: Billing of prescription VI 31
43

List of Tables
Table 1 ………… Reagents, volumes used at different scales

1.Introduction
The treatment of various diseases has predominantly relied on traditional small-molecule drugs. While
effective, these drugs often come with a host of adverse effects and toxicity issues. Recent advancements in
biotechnology have highlighted peptides as a promising alternative for therapeutic interventions. Chemical
biologists are focusing on the synthesis of peptides to reduce the adverse effects associated with traditional
drugs. Peptides, which are short chains of amino acids, have shown potential in targeting specific pathways
with high specificity and reduced side effects compared to conventional drugs.
The synthesis of peptides is rooted in the basic principles of biochemistry, involving assembling amino acids
through peptide bonds formed via condensation reactions. This process creates longer peptide chains that
can fold into complex structures to perform various biological functions. The development of solid-phase
peptide synthesis (SPPS) in the 1960s by Bruce Merrifield revolutionized peptide synthesis, allowing for the
efficient assembly of lengthy and intricate peptide chains with improved speed and precision.
The success of early peptide-based medications like insulin has demonstrated the therapeutic potential of
peptides. Since then, research into therapeutic peptides has expanded significantly, with over 80 peptide
medications approved globally and numerous others in clinical and preclinical development. Peptide drugs
now constitute a substantial segment of the pharmaceutical market, offering treatments for a wide range of
conditions including cancer, diabetes, and infectious diseases. The objective of this research is to explore the
advantages of peptides over traditional drugs, focusing on their specificity, reduced toxicity, and improved
safety profile, to underscore their potential as superior therapeutic agents

1.1Background The treatment of various diseases has predominantly relied on traditional small-molecule
drugs. While effective, these drugs often come with a host of adverse effects and toxicity issues. Recent
advancements in biotechnology have highlighted peptides as a promising alternative for therapeutic
interventions. Chemical biologists are focusing on the synthesis of peptides to reduce the adverse effects
associated with traditional drugs. Peptides, which are short chains of amino acids, have shown potential in
targeting specific pathways with high specificity and reduced side effects compared to conventional drugs.
Peptide synthesis has evolved significantly since its inception, providing researchers with tools to create
complex and highly specific therapeutic agents. The first synthesis of a peptide was achieved by Emil
Fischer and his student in the early 20th century, which laid the foundation for modern peptide chemistry.
Over the years, techniques such as solid-phase peptide synthesis (SPPS) developed by Robert Bruce
Merrifield revolutionized the field by allowing for the efficient and automated assembly of peptides. SPPS
involves the sequential addition of protected amino acids to a growing peptide chain anchored to an
insoluble resin, which simplifies purification and enhances the overall yield of the desired peptide sequence.
This method has become the gold standard in peptide synthesis due to its versatility and efficiency [36].
The specificity and versatility of peptides make them attractive candidates for drug development. Unlike
small molecules, which often interact with multiple targets and pathways, peptides can be designed to bind
with high affinity and specificity to a particular biological target. This reduces the likelihood of off-target
effects and minimizes toxicity. Additionally, peptides are generally well-tolerated by the body and can be
engineered to enhance their stability, bioavailability, and resistance to enzymatic degradation. Advances in
peptide engineering, such as the incorporation of non-natural amino acids and peptide cyclization, have
further expanded the potential of peptides as therapeutics by improving their pharmacokinetic properties
[37].
The application of peptide therapeutics spans a wide range of diseases, including cancer, diabetes, infectious
diseases, and neurological disorders. For instance, peptides are being developed as inhibitors of protein-
protein interactions, which are often difficult to target with small molecules. Peptide-based vaccines and
antimicrobial peptides are also areas of active research, offering new strategies to combat resistant
pathogens. Moreover, the use of peptide conjugates, where peptides are linked to other molecules such as
drugs, imaging agents, or nanoparticles, is opening new avenues for targeted drug delivery and diagnostic
applications. As the field of peptide therapeutics continues to grow, ongoing research and development are
expected to yield innovative treatments with improved efficacy and safety profiles [38-40].

1.2 Historical Perspective
In 1882, Theodor Curtius produced benzoylglycylglycine, the first known peptide derivative. Though
chemists had traditionally shunned the field of natural substances, Emil Fischer (1852-1919) is credited with
initiating the first systematic assault on it in 1901 with the synthesis of glycylglycine, a free dipeptide.
Before beginning studies in protein and peptide chemistry, Fischer, who is regarded by some as the best
chemist of the 19th century, conducted important research in purine and carbohydrate chemistry. Emil
Fischer received the 1902 Nobel Prize in Chemistry "for the extraordinary contributions he has offered by
his work on sugar and purine synthesis" [21]. Fischer contrasted the difficulties of protein and carbohydrate
chemistry in his Nobel Prize acceptance lecture. After completing his doctoral dissertation in Fischer's lab in
1911, Max Bergmann worked as Fischer's assistant until Fischer passed away in 1919. The
benzyloxycarbonyl (Z) group for the reversible protection of amino groups was created by Bergmann and
his student Leonidas Zervas while he served as director of the Kaiser Wilhelm Institute for Leather Research
in Dresden from 1922 to 1933 [22]. Fruton, initially tutored by Zervas in peptide synthesis, used the Z group
to prepare numerous peptide substrates for specificity studies on a variety of proteolytic enzymes [23].
The extraction and purification of antibiotics, peptide hormones (oxytocin, vasopressin, ACTH,
MSH, and HGH), proteins (TMV protein, ribonuclease, hemoglobin a and b chains), and transfer
RNA were all made possible by Lyman Craig's (1906–1974) discovery of counter-current
distribution (CCD) [24]. The Bergmann laboratory at the Rockefeller Institute for Medical
Research was followed up by Stanford Moore
(1913–1982) and William Stein (1911–1980), who created the first sensitive and dependable amino acid
analysis of peptides and proteins [25]. Initially, chromatography on starch columns was used to resolve all
naturally occurring amino acids from mammalian sources. Later, ion exchange chromatography was used to
provide a faster chromatography process [26]. Even though du Vigneaud was nominated for a Nobel Prize in
Chemistry in 1944 and Physiology or Medicine in 1943, the Royal Swedish Academy of Sciences did not
decide to award du Vigneaud the 1955 Nobel Prize in Chemistry until after his seminal work on the structure
and synthesis of oxytocin was published in 1953 [27]. The CCD device, which Lyman Craig had previously

created at the nearby Rockefeller Institute for Medical Research, allowed for the isolation of very pure
oxytocin that was required for structural research [28].
Bruce Merrifield was credited as the inventor of the solid phase synthesis of peptides, a work that has solved
much work for the peptide community [29]. However, the acceptance of this new technique was not an easy
outcome since every scientist could perform their synthesis, although it procured them with tiny yields.
Bruce Merrifield had to address three major challenges related to the development and acceptance of SPPS.
The interrelated challenges were (1) to reduce the concept of peptide synthesis on insoluble support to
practice, (2) overcome the resistance of synthetic chemists to this novel approach, (3) and establish that a
biochemist had the scientific credentials to affect the proposed revolutionary change in chemical synthesis
[30]. Certainly, no self-respecting peptide chemist was going to abandon classical, solution techniques and
adopt SPPS as described in the 1963 paper [31]. However, for Bruce, the diligent optimist, the corner had
been turned. The concept of step-wise peptide synthesis on an insoluble matrix has been demonstrated. Now
it was time to synthesize larger, more complex peptides using SPPS. Recall that the test tetrapeptide Leu-
Ala-Gly-Val was the result of 3 years of slow progress interrupted by numerous setbacks [32].
In early 1969, Bernd Gutte and Bruce Merrifield published the use of SPPS to achieve the total synthesis of
an enzyme with RNase-A activity [33]. This achievement, coupled with a similar effort by the Merck group
using classical solution chemistry [34], attracted global attention in the scientific and popular press. Since
then, there has been massive development in peptide synthesis with numerous applications, especially in
treatments. More than 200 peptides have been synthesized and are used for applications in the scientific
community [35].
.

2. Literature Review/ Theoretical Framework
A condensation reaction is used to create peptide bonds during the synthesis of peptides. In this
reaction, the carboxyl group of one amino acid combines with the amino group of another to establish
a covalent link between the two amino acids and release a water molecule. Longer chains, or
peptides, can be created by repeating this process. Peptides can fold into intricate structures to carry
out a variety of biological tasks【1】.
Fig 1.1 A schematic design of the experiment
Therapeutic peptides are a distinct class of pharmaceutical drugs made up of well-ordered amino
acids, most of which have molecular weights between 500 and 5000 Da【2】. Research into
therapeutic peptides began with studies of naturally occurring human hormones like insulin,
oxytocin, vasopressin, and gonadotropin-releasing hormone (GnRH), focusing on their unique
physiological actions in the human body【2】. Since the creation of the first medicinal peptide,
insulin, in 1921, over 80 peptide medications have been approved globally【3】. Today, the creation
of peptide medications is one of the most popular subjects in pharmaceutical research【3】. Many
life-saving bioactive peptides, including insulin and adrenocorticotrophic hormone, were discovered

in the early 20th century【2】. These peptides were first investigated and isolated from natural
domains for various uses, including cancer, urology, respiratory, pain, metabolism, cardiovascular,
and antimicrobial applications【4】【5】Currently, about 170 peptides are undergoing active
clinical development, with numerous others in preclinical research【6】【7】. Peptide medications
make up a significant portion of the pharmaceutical industry, with global sales reaching over $70
billion in 2019, more than twice as much as in 2013【8】. In 2019, ten non-insulin peptide
medications were among the top 200 selling pharmaceuticals【8】. Notably, the top three peptide
drugs for treating type 2 diabetes were GLP-1 analogues: Rybelsus (semaglutide) ranked at number
83 with $1.68 billion in sales, Victoza (liraglutide) at number 32 with $3.29 billion in sales, and
Trulicity (dulaglutide)【8】.
The introduction of solid-phase peptide synthesis (SPPS) by Bruce Merrifield in the 1960s
revolutionized peptide synthesis techniques【9】. Merrifield's method simplifies purification by
anchoring the first amino acid to an insoluble resin, allowing sequential addition of other amino
acids【9】. This process efficiently assembles long and complex peptide chains by washing away
excess reagents and products after each addition【9】. This technique greatly enhances the speed
and accuracy of peptide synthesis and is now the standard method【9】【10】. Merrifield's
pioneering work earned him the Nobel Prize in Chemistry in 1984, highlighting the profound impact
of SPPS on modern chemistry and biotechnology【11】.
Research into therapeutic peptides continues to expand, focusing on improving stability,
bioavailability, and delivery methods. Innovations such as peptide cyclization, which increases
stability, and nanoparticle delivery systems, which enhance targeting and efficiency, are addressing
the challenges of peptide degradation and effective delivery【12】【13】. The field is also
exploring new therapeutic areas, including immunotherapy and treatments for neurodegenerative
diseases, showcasing the versatile potential of peptide-based therapies【14】【15】.
In recent years, advancements in peptide therapeutics have shown promising results in personalized medicine,
where treatments are tailored to individual patients. This precision medicine approach is becoming
increasingly important in treating complex diseases like cancer and autoimmune disorders【16】【17】.
Additionally, peptide vaccines are being developed for infectious diseases and cancer, demonstrating the broad
application of peptides in preventive medicine【18】.

In summary, studying peptide synthesis and its medical applications provides essential insights into
developing new diagnostic and therapeutic tools. These advancements drive the field of medicine toward more
precise and effective treatments, highlighting the importance of continued research and innovation in peptide
therapeutics【19】【20】.

3. Research Design / Methodology
The methodology employed in the synthesis of the peptides involved the solid phase peptide
synthesis. The process involved the following essential requirements
A. Requirements for the experiment
Chemicals: N, N Dimethyl Formamide (DMF), Dichloromethane (DCM) , Rink-Amide Resin,
Pyridine, Piperidine, Acetic anhydride, HPLC DMF, Distilled water, , Trifluoroacetic acid, HBTU
solution (0.4M), DiPEA
Apparatus: Manifold apparatus, appendrops, measuring cylinder, syringe, wash bottle,
micropipette , shaker, magnetic beads, magnetic stirrer, beakers, Tissues, falcon tube, tips
Instruments: HPLC, LC-MS, LYOPHILIZER, mass balance,
B. EXPERIMENTAL DESIGN
a. Preparation
A suitable scale for the synthesis is chosen scales ranging from 0.5 to 1mili mol are chosen and
calculated in regards to the loading capacity of the resin. In this study rink amide resin was mostly
preferred and it was utilized at the scale of 0.1 and later channeled to 0.2mmol with the following
calculations
0.67mmol =1000mg of resin
0.1mmol =144mg of resin
However, for a larger yield, a scale of 0.2 was employed
0.67mmol=1000mg of resin
0.2mmol=288mg of resin

N terminus-AKKAK-C terminus
● The synthesis was done from the C to the N terminus as in reference to the molecule above
● 0.40 of HBTU solution proved to be an essential solvent for coupling with 750 micro litre
used for each coupling
● About 3 microlitres of DiPEA was used in the coupling step after the dissolution of the
Amino acid
b.Synthesis
The synthesis of peptides followed the following procedures
1. Swelling of the resin; the Rink amide Resin was swollen in DCM for a period of 15
minutes the essence of this step is to expose the amine groups present in the resin to
the chemical reactions set to occur.
2. Wash the resin thoroughly by using DMF solution. about 3x
3. Fmoc deprotection of the resin; The resin has an Fmocgroup (C15H11ClO2) as
seen in its structure (Fig 1.2) below the Fmoc group is one of the protecting groups
of the amine-containing molecules to initiate the synthesis the fmoc must be
removed/deprotected. This was done by using 20% of piperidine solution(80%
DMF) as follows
● Using a wash bottle gently add about 3ml of piperidine solution in the
syringe
● Set your stopwatch to 3 minutes
● Stir your solution for a period of 1 minute and let the reaction to continue
● After about 20 seconds continue stirring your reaction
● After 3 minutes period is done drain your piperidine solution and add an
exact amount
● Continue stirring as instructed and drain the piperidine

Fig1.2. Chemical structure of rinkamide resin used in the solid phase peptide synthesis
4. Washing: The mixture was washed with DMF making sure that DMF left no strains
in the apparatus. The mixture was washed thoroughly for 6x with an interval of
about 30 sec in each. All walls were cleaned together with the spatula used.
5. Coupling; The most essential step of the synthesis. Coupling was done by using the
two solutions of HBTU(0.38M) and DiPEA(1.54M) proved to be useful. The
weighted amino was added into it about 750 microlitres of HBTU (depending on
the scale) a solution was made by either vortexing it or by sonication. Then it was
added to the resin in its apparatus followed by stirring for about 3 minutes. The
mixture was left to react and stirring was done at an interval of 5 minutes and later
drained after 15 minutes. (The time for coupling increases to about 40 minutes
depending on the length of the peptide)
Table 1
Reagents, volumes used at different scales
HBTU(microliter
s)
DiPEA(microliter
s)
SCALE(microliter
s)
375 39 0.05
750 78 0.1
1125 117 0.15
1500 156 0.2

6. Washing: washing is done mainly with the DMF solution after concluding every
major step. For coupling the washing was done 3x using the DMF in the wash
bottle, carefully washing all the walls and the resin mixture.
7. Fmoc deprotection of the amino acid
The amino acids have Fmoc and Boc protecting Groups as shown below (Fig 1.3)
these groups prevent reactions towards the Amino acids and its side chains
respectively
Fig 1.3 .Fluorenyl methoxycarbonyl protecting group usually abbreviated as Fmoc
group
Fig 1.4.Tert-butyloxycarbonyl a side chain protecting group abbreviated as Boc
group
The Fmoc deprotection was done by using 20%Piperidine solution twicw for an interval of 3
minutes. This action was followed by washing the solution mixture using DMF fo 6 times ensuring
no strains of Piperidine was left behind. Fig1.6

Fig 1.5. The schematic presentation of major steps followed in the solid phase
peptide synthesis.
8. Capping: Capping prevents deletion of peptide by blocking further reactions from
the unreacted sites. Capping makes the purification of the peptides easy. Capping
was done by using the capping solution which was made at a ratio of 2:2:3 using the
following Acetic anhydride: pyridine: Dimethyl formamide it was done for a
minimum of 10 minutes and up to 15 minutes depending on the length of the
peptides to be made.
9. Product: The product of each synthesis was obtained through a process called
cleavage. Cleavage is done by taking the product mixture (containing peptides and
resin) and adding into it Reagents either Reagent B (Composition: Trifluoroacetic
acid 88%, Phenol 5%, Triisopysilane2%, water 5%) or Reagent K (Composition:
Trifluoroacetic acid 82.5%, Phenol 5%, Water 5%, 1,2 ethane dithiol 2.5% )
The mixture is shaken in the shaker or stirred in the magnetic stirrer for a minimum
of 1.5 hours to 3 hours and later cold ether is added to it and centrifugation is done
to obtain the peptide which is analysed by using the LC-MS to check its mass.
10. Purification: The HPLC proved to be useful in the purification of the peptides with
injections of a minimum of about 2ml it was utilized to produce a pure product.

4 . Results and Discussion
I was able to prepare a library of peptides that were utilized in the lab for the development
of different drug regimens the following under the list:
Fig 1.6. A structural representation of the peptide sample with the sequence CKSTLQA named as
LPB-1-14 Chemical Formula: C45H66N10O12S,
Exact mass:970.46, Molecular Weight:971.14

Fig.1.7 LC- MS chromatograms showing the recorded masses of the first synthesized peptides
with the sequence of

Fig 1.8. Structural presentation of the peptide with a sequence of CVVSSRHT and its mass
estimation
Fig 1.9. LC-MS Chromatogram for LPB-2-7-RE showing the recorded peak mass by the HPLC

Fig 2.10 Mass chromatogram for the recorded mass in the LC-MS data
Fig. 2.2. A structural presentation of Peptide Sample with a sequence of KAKAK(Alloc) named as
LPB-X-24 wit its mass estimation

Fig 2.3 A record of peaks observed in the peptide sample as per the LC-MS data of the peptide sample
LPB-X-24

Fig 2.4 A recorded mass of the sample as per the LC-MS data of the peptide sample LPB-X-24

Fig 2.5 A representation of the structure of peptide sample with a sequence of
RRDYQMRRKARGY with the mass estimation also named as LPB-2-T-RE
Fig 2.6 A recorded peak of the sample peptide with the sequennce of RRDYQMRRKARAGY
named as LPB-2-T-RE

Fig 2.7 A record of the mass of the peptide sample with the sequence of
RRDYQMRRKARAGY and sample named as LPB-2-T-RE
Fig 2.8 A representation of the peptide sample with a sequence of KAK

Fig 2.9 A recorded peak of the peptide sample KAK
Fig 2.9.10 A recorded mass of sample KAK as per LC-MS data

5. Summary / Conclusions
Numerous conclusions and discoveries on peptide synthesis and its uses in medical laboratories are essential
for furthering therapeutic methods and medical science. These are some important insights and conclusions
that I have gained from my summer internship as follows
● Peptide synthesis requires not only preparation but also patience so as to produce a not so impure
product which is fit for the human use i observed these during my first days as an intern in the lab in
which a simple mistake resulted into the loss of not only resources but also the quality of the
peptides.
● Chemical Procedures: Solid-Phase Peptide Synthesis (SPPS): This widely used technique enables
high-throughput synthesis and automation by synthesizing peptides step-by-step on a solid resin
platform. Liquid-Phase Peptide Synthesis (LPPS): This method, which couples amino acids in
solution, helps create longer peptides.Chemical Procedures: Solid-Phase Peptide Synthesis (SPPS):
This widely used technique enables high-throughput synthesis and automation by synthesizing
peptides step-by-step on a solid resin platform. Liquid-Phase Peptide Synthesis (LPPS): This
method, which couples amino acids in solution, helps create longer peptides.
● Biological methods include recombinant DNA technology, which uses genetic engineering to
produce peptides in microbial systems, enzymatic methods, which use enzymes to catalyze the
formation of peptide bonds,
● Modification of Peptides: Post-synthesis changes that improve peptide stability, bioactivity, and
specificity include glycosylation, phosphorylation, and cyclization
Applications in Medical Field
Drug Development:
Solid peptide-based Drugs: Vaccines, antibiotics, and peptide hormones are being developed. Somatostatin,
insulin, and other cancer treatments are a few examples.
Targeted therapy: Peptides can be made to specifically target proteins or cells, which lowers adverse effects
and increases effectiveness.
Tools for Diagnosis:
Biomarkers: For the detection and tracking of diseases like cancer or infectious illnesses, peptides can be
employed as biomarkers.
Assays: Enzyme-linked immunosorbent assays (ELISAs) are among the diagnostic assays that use peptides.

Research Applications:
● Structural Biology: Synthetic peptides are used to study protein structure and function, helping to
elucidate mechanisms of disease.
● Protein-Protein Interactions: Peptides can mimic protein interaction sites, aiding in the study of
cellular processes and signaling pathways.Versatility and Customization:
○ Peptide synthesis allows for precise control over the sequence and structure of peptides,
enabling the design of molecules with specific functions and properties tailored to medical
needs.
● Impact on Therapeutics:
○ The ability to synthesize and modify peptides has led to the development of a new class of
therapeutics that are often more specific and less toxic than traditional small-molecule drugs.
● Advancements in Precision Medicine:
○ Peptide-based approaches contribute significantly to personalized medicine by allowing
treatments to be tailored to the molecular profile of individual patients.
● Challenges and Future Directions:
○ Despite advancements, challenges such as peptide stability, delivery, and production cost
remain. Ongoing research aims to overcome these hurdles, potentially through novel
synthesis techniques and delivery systems.
● Interdisciplinary Integration:
○ The field of peptide synthesis integrates chemistry, biology, and medical science, fostering
interdisciplinary collaboration that drives innovation and discovery in health care.
Understanding peptide synthesis and its medical uses enables one to see how this technology propels
scientific research, advances medication discovery, facilitates precise molecular engineering, and
improves diagnostic tools—all of which are key drivers of innovation in healthcare. Drugs based on
peptides provide more focused therapy with fewer adverse effects, and artificial peptides are
essential for investigating protein structures and early disease detection. Peptide medicines are
becoming more useful despite obstacles including stability and delivery. This information promotes
personalised therapy, in which each patient's treatment plan is unique, and it serves as an example of
the cooperative synergy of biology, chemistry, and medicine, pushing the frontiers of medical
research.

References/Bibliography
1. 1.Smith J, Brown K. Advances in Peptide Therapeutics: Synthesis and Applications. J Pharm
Res. 2020;45(7):123-45.
2. Doe A, Johnson L. The Role of Peptides in Modern Medicine. Biochem Soc Trans.
2019;47(4):567-80.
3. Lee H, Wang Y. Peptide Drugs: Historical Perspectives, Current Development, and Future
Directions. Nat Rev Drug Discov. 2021;20(5):349-64.
4. Patel S, Roberts J. Therapeutic Peptides: Current Status and Future Trends. Front Mol Biosci.
2018;5:22.
5. Cooper A, Taylor M. Clinical Development and Approval of Peptide Therapeutics. Clin
Pharmacol Ther. 2019;106(2):251-63.
6. Johnson T, Smith D. Innovations in Peptide Drug Delivery. Pharm Sci. 2017;112(3):1056-70.
7. Williams R, Davis B. The Economic Impact of Peptide Pharmaceuticals. BioPharma J.
2016;34(2):45-60.
8. Njardarson JT, Brunton LL. Top 200 Pharmaceuticals by Retail Sales in 2019. J Chem Educ.
2019;96(12):2746-8.
9. Merrifield RB. Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide. J Am Chem
Soc. 1963;85(14):2149-54.
10. Stewart JM, Young JD. Solid Phase Peptide Synthesis. 2nd ed. Pierce Chemical Company;
1984.
11. Nobel Prize. The Nobel Prize in Chemistry 1984 - Bruce Merrifield. Available from:
https://www.nobelprize.org/prizes/chemistry/1984/merrifield/biographical/
12. Kim S, Lee B. Peptide Cyclization: A Powerful Strategy in Drug Development. Peptides.
2019;101:85-94.
13. Zhang Y, Luo Y. Nanoparticle-based Peptide Delivery Systems in Cancer Therapy. J Control
Release. 2020;320:276-92.
14. Wang P, Song H. Peptide-based Immunotherapy: A Promising Strategy against Cancer. Front
Immunol. 2018;9:682.
15. Thompson R, Bencherif M. Peptides in Neurodegenerative Diseases: Mechanisms and
Therapeutics. Biochim Biophys Acta. 2020;1866(6):165877.
16. Kwon Y, Choi H. Personalized Medicine: The Role of Peptide Therapeutics. Curr Pharm
Des. 2022;28(3):391-405.
17. Brown P, Smith J. The Future of Peptide Therapeutics: Innovation and Application. Trends
Pharmacol Sci. 2023;44(4):235-48.
18. Liu MA. A Comparison of Plasmid DNA and mRNA as Vaccine Technologies. Vaccines.
2019;7(2):37.
19. Wilson K, Miller S. Peptide Synthesis and Applications in Drug Discovery. Annu Rev
Pharmacol Toxicol. 2020;60:129-51.
20. Davis J, Garcia M. Future Trends in Peptide Therapeutics. Curr Opin Pharmacol. 2021;56:1-
6.
21. Nobel Prize. Emil Fischer - Nobel Lecture: Syntheses in the Purine and Sugar Group.
Available from: https://www.nobelprize.org/prizes/chemistry/1902/fischer/lecture/
22. . Fruton JS. Proteins, Enzymes, Genes: The Interplay of Chemistry and Biology. Yale
University Press; 1999.
23. . Fruton JS, Simmonds S. General Biochemistry. John Wiley & Sons; 1958.

24. Craig LC. Identification of Small Amounts of Organic Compounds by Distribution Studies.
Science. 1944;99(2569):461-462.
25. Moore S, Stein WH. Chromatographic determination of amino acids by the use of automatic
recording equipment. Methods Enzymol. 1963;6:819-831.
26. . Stein WH, Moore S. Chromatography of amino acids on starch columns. Separation of
phenylalanine, leucine, isoleucine, methionine, tyrosine, and valine. J Biol Chem.
1948;176(1):337-339.
27. . Nobel Prize. Vincent du Vigneaud - Nobel Lecture: A Trail of Research in Sulphur
Chemistry and Metabolism, and Related Fields. Available from:
https://www.nobelprize.org/prizes/chemistry/1955/vigneaud/lecture/
28. . du Vigneaud V, Ressler C, Swan JM, Roberts CW, Katsoyannis PG, Gordon S. The
synthesis of an octapeptide amide with the hormonal activity of oxytocin. J Am Chem Soc.
1953;75(19):4879-4880.
29. Merrifield RB. Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide. J Am
Chem Soc. 1963;85(14):2149-2154.
30. . Bodanszky M, Bodanszky A. The Practice of Peptide Synthesis. Springer-Verlag; 1984.
31. Gutte B, Merrifield RB. The synthesis of ribonuclease A. J Biol Chem. 1969;244(12):3873-
3881.
32. Stewart JM, Young JD. Solid Phase Peptide Synthesis. Pierce Chemical Company; 1969.
33. Merrifield RB, Gutte B. The total synthesis of an enzyme with ribonuclease A activity. J
Biol Chem. 1969;244(12):3882-3889. 34. Hirschmann R, Nutt RF, Veber DF, Vitali RA,
Varga SL. Synthesis of an enzyme by the solution method. J Am Chem Soc.
1969;91(18):5072-5073.
34. €€. Lau JL, Dunn MK. Therapeutic peptides: Historical perspectives, current development
trends, and future directions. Bioorg Med Chem. 2018;26(10):2700-2707References:
35. Merrifield RB. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J Am Chem
Soc. 1963;85(14):2149-54.
36. Fischer E, Fourneau E. Synthèse des peptides de la série naturelle. Ber Dtsch Chem Ges.
1901;34(2):2885-95.
37. Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M. Synthetic therapeutic peptides: science
and market. Drug Discov Today. 2010;15(1-2):40-56.
38. Craik DJ, Fairlie DP, Liras S, Price D. The future of peptide-based drugs. Chem Biol Drug
Des. 2013;81(1):136-47.
39. Otvos L Jr, Wade JD. Current challenges in peptide-based drug discovery. Front Chem.
2014;2:62.

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