The document discusses protein and peptides, including their structure and stability problems. It describes the primary, secondary, tertiary, and quaternary structure of proteins. Issues like denaturation, adsorption, aggregation, and precipitation are explained as stability problems for proteins and peptides. The conclusion emphasizes the need for viable delivery systems to efficiently deliver proteins and peptides in biologically active forms through non-parenteral routes.

1. PRESENTED BY:
TALPE SHUBHAM MARUTI
M.PHARM SEM-II
(PHARMACEUTICS)
SUBJECT:-NOVEL DRUG DELIVERY SYSTEMS
.
AMRUTVAHINI SHETI AND SHIKSHAN VIKAS SANSTHA’S
AMRUTVAHINI COLLEGE OF PHARMACY,
SANGAMNER 422 608
Physical Aspects, Biochemistry
of Protein & Peptide.

2. CONTENT..
 Protein & Peptides
 Structure of protein
 Properties
 Stability problems
 Conclusion
 References
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3. Protein & Peptides
 PROTEINS: Proteins are the large organic compounds made of
amino acids arranged in a linear chain and joined together by
peptide bonds.
Protein > 50 amino acids
 PEPTIDES: These are short polymers formed from the linking,
in a defined order of amino acids.
peptide < 50 amino acids
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4. Structure of protein
a) Primary structure:
b) Secondary structure:
- alpha-helix
- beta-pleated sheets
c) Tertiary structure:
d) Quaternary structure:
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5.  a) Primary structure:
The linear sequence of amino acids in a
polypeptide chain.
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6.  b) Secondary structure:
i) Alpha-helix
- Three dimensional arrangement of amino acids with the
polypeptide chain in a cork screw shape.
ii) Beta-pleated sheet
- Polypeptide chains are arranged side by side.
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7.  c) Tertiary structure:
The overall three dimensional shape of a polypeptide
chain.
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8.  d) Quaternary structure:
The combination of two or more tertiary polypeptides
that makes up a protein.
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10. Properties
 The Protein are the most abundant biological and
organic molecule they are soluble in water and it can
formed a Colloidal solution with water.
 Physicochemically and Metabolically Stable System.
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11. Stability problems
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12. Denaturation
 Denaturation refers to any nonproteolytic modification of the
unique structure of a native protein that affects definite
changes in physical, chemical and biological properties.
 Denaturation leads to rearrangement and loss of quarternary
and tertiary structure and the hydrophobic and hydrogen
bonds are broken.
 Conditions include:
 Solvent changes
 pH change
 Alteration in ionic strength
 Temperature rise
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13. Adsorption
 Proteins and peptides tend to absorb at interfaces such
as air-water and air-solid.
 This leads to conformational rearrangement which may
cause loss or change in the biological activity.
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14. Aggregation and Precipitation
 Mechanism of protein aggregation involves protein
denaturation and noncovalent association via hydrophobic
residues.
 Aggregation on a macroscopic scale leads to precipitation.
 Conditions favour include:
 Large air-water interface
 Agitation of the solution
 Presence of large headspace within the confines of
container.
 Increase in thermal motion of the molecules due to
agitation.
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15. CONCLUSION
 This poses an urgent challenge to the pharmaceutical
industry to develop viable delivery systems for the
efficient delivery of these complex therapeutic in
biologically active form.
 Much work needs to be done on the development of
viable delivery systems for non parenteral
administration to make peptide and protein
pharmaceuticals commercially viable and
therapeutically useful.
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16. REFERENCES
 Controlled drug Delivery Concepts and Advances By
Vyas, Roop Khar, Proteins and Peptides Delivery
Considerations Page No: 503-511.
 Advances in Controlled and Novel Drug Delivery By
N.k.Jain, Oral delivery of protein and peptides Page no:
232-235.
 Drug Stability Principles and practices By J.Carstensen,
Stability of Polypeptides and Proteins Page no:560-572
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