Creative Peptides has successfully developed a reliable method for the analysis of peptides by using several of the peptide analysis methods.

1. Analytical Method Development and Validation
Peptides are widely found in nature and have important physiological
effects on the human body. In recent years, with the vigorous
development of life science research, the research progress on
peptides is changing with each passing day. Peptides have shown
magical research and application value in immune function,
information transmission, cell secretion, precursor signal, disease
occurrence and treatment.
Introduction to Detection Methods
Currently, high performance liquid chromatography (HPLC), capillary
electrophoresis (CE), mass spectrometry (MS) and their associated
technology have become a primary means of measuring the peptide,
and are being more widely used.
High performance liquid chromatography (HPLC)
HPLC is a new separation and analysis technology developed on the
basis of classical liquid chromatography and gas chromatography. It
has the characteristics of high separation efficiency, high speed, easy
operation, good detection sensitivity and wide application range to
samples. It has been widely used for the analysis and determination
of peptides. Reversed-phase high performance liquid
chromatography (RP-HPLC) has a very high resolution for the
analysis and purification of non-polar small molecule peptides with a
molecular mass below 1000.
Capillary electrophoresis (CE)
CE is a kind of liquid phase separation technology that uses a
high-voltage electric field as a driving force and a capillary as a
separation channel to separate components according to the
difference in mobility and distribution between components in a
sample.
Mass spectrometry (MS)
The mass spectrum of a peptide detected by mass spectrometry (MS)

2. is usually referred to as a fingerprint. The biggest advantage of mass
spectrometry is stability, reproducibility and high accuracy. At present,
mass spectrometry is applied to peptide detection mainly by
matrix-assisted laser desorption time-of-flight mass spectrometry
(MALDI-TOF-MS), liquid chromatography-mass spectrometry (LC-MS)
and capillary electrophoresis-mass spectrometry (CE-MS).
Hydrophobic interaction chromatography (HIC)
HIC is the use of a hydrophobic group in a peptide to create a
hydrophobic interaction with a stationary phase for separation
analysis. Iron-Exchange chromatography (IEXC) can be used to
isolate and purify biologically active peptides under neutral conditions
using different chargeability of the peptide. Methods for detection of
peptide analysis also include chromatography of membrane protein
(CMP), high-performance displacement chromatography (HPDC),
perfusion chromatography (PC), affinity chromatography (AC).
In addition to the above methods, amino acid composition analysis,
amino acid sequence analysis, field analytical mass spectrometry, IR,
UV spectroscopy, CD, circular dichroism, bioassay, radioisotope
labeling and immunological methods have been applied to analyze
the peptides characterization.
Our Services
 Extraction of peptides: protease inactivation
 Pretreatment: removal of protein
 Peptide purification: chromatography, capillary gel
 Peptide identification: MALDI-TOF-MS, LC-MS, CE-MS
 Peptide quantification: immunoassay, isotope mass shift
By removing all proteins in biological samples, body fluids, and tissue
extracts by size exclusion chromatography, LC-MS-based assays can
be quickly established and validated to identify peptides with high
precision and repeatability. After a detailed and comprehensive
discussions with customers, we will provide you with a peptide set
research and analysis services tailored.

3. Creative Peptides has successfully developed a reliable method for
the analysis of peptides by using several of the peptide analysis
methods mentioned above. Creative Peptides is dedicated to the
detection and analysis of peptides and provides a powerful tool for
research in the fields of protein chemistry such as medicine, clinical
pathology and preventives.
References:
1. Schmid, I., Bonnington, L., Gerl, M., Bomans, K., Thaller, A. L.,
Wagner, K., ... & Hasmann, M. (2018). Assessment of susceptible
chemical modification sites of trastuzumab and endogenous human
immunoglobulins at physiological conditions. Communications
Biology, 1(1), 28.
2. Kaneko, N., Yoshimori, T., Yamamoto, R., Capon, D. J., Shimada,
T., & Sato, T. A., et al. (2013). Multi epitope-targeting
immunoprecipitation using f(ab') fragments with high affinity and
specificity for the enhanced detection of a peptide with
matrix-assisted laser desorption ionization-time-of-flight mass
spectrometry. Analytical Chemistry, 85(6), 3152-3159.
3. Gilg, D., Riedl, B., Zier, A., & Zimmermann, M. F. (1996). Analytical
methods for the characterization and quality control of pharmaceutical
peptides and proteins, using erythropoietin as an example. Pharm
Acta Helv, 71(6), 383-394.