Related Experiment Video
Updated: Jun 24, 2026
08:48
Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
Published on: January 26, 2016
Cyclic Peptides with RNase A Inhibitor Activity Based on Amino Acid Sequences Screened from the Fv-Antibody Library
Jeong Soo Sung1, Hye-In Kim1, Hyun-Woo Song1
1Department of Materials Science and Engineering, Yonsei University, 50 Yonsei-Ro, Seodaemun-Gu, Seoul 03722, South Korea.
ACS Biomaterials Science & Engineering
|June 22, 2026
Summary
Cyclic peptides derived from antibody fragments show enhanced inhibition of Ribonuclease A (RNase A). Cyclization improves metabolic stability and inhibitory activity, supporting their development as novel RNase A inhibitors.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Ribonuclease A (RNase A) degrades single-stranded RNA, necessitating effective inhibitors for RNA protection.
- Fv-antibodies, comprising complementarity-determining regions (CDRs) and framework regions (FRs), are explored for RNase A inhibition.
Purpose of the Study:
- To synthesize and evaluate cyclic peptides derived from RNase A-inhibitory CDR3 sequences.
- To enhance the metabolic stability and inhibitory activity of RNase A inhibitors.
Main Methods:
- Screening of an Fv-antibody library to identify RNase A inhibitory CDR3 sequences.
- Synthesis of cyclic peptides via N- and C-terminal cysteine incorporation for disulfide bond formation.
- Assessing metabolic stability using liver microsome assays and inhibitory activity via cCMP hydrolysis, fluorescence, and RNA cleavage assays.
- Computational docking simulations to analyze peptide conformation-activity relationships.
Main Results:
- Cyclization significantly increased the metabolic stability (half-life) of CDR3 peptides.
- Cyclic peptides demonstrated superior RNase A inhibitory activity compared to Fv-antibodies and linear peptides.
- Docking simulations provided insights into the conformational effects on inhibitory function.
Conclusions:
- Cyclization is an effective strategy to enhance the metabolic stability and inhibitory potency of RNase A-inhibitory CDR3 sequences.
- Cyclic peptides represent a promising platform for developing novel and effective RNase A inhibitors.
