# Peptide Mimics of the Collagen Triple Helix

> **NIH NIH R01** · UNIVERSITY OF PENNSYLVANIA · 2022 · $494,602

## Abstract

Project Summary/Abstract
Protein-protein interactions (PPIs) are involved in a diverse array of critical biological processes,
including cell proliferation, growth, differentiation, and apoptosis. To date, there is no general way to
modulate collagen protein-protein interactions, and many fundamental aspects of biomolecular
recognition are still unknown. Specifically, numerous interactions between collagen triple helices and
proteins are not fully characterized or understood. We have recently shown that collagen aza-peptides
in which at least one alpha-carbon atom has been substituted with nitrogen, have additional interstrand
hydrogen bonds in their collagen triple helix, resulting in hyperstability and more efficient self-assembly.
As a result, even short collagen aza-peptides reliably self-assemble into thermostable triple helices,
making them a promising choice for novel triple helix mimics. With this project, we propose to use
minimal aza-peptides to create linear and cyclic collagen peptide triple helix mimics. Our specific aims
are as follows: 1) Synthesize and characterize hyperstable synthetic mimics of collagen peptides; 2)
Synthesize and characterize cyclic collagen peptide triple helix mimics (CCP-mimics); 3) Characterize
protein interactions our synthetic collagen peptides. Aza-peptides will be synthesized using solid-phase
peptide synthesis (SPPS) in order to introduce aza-amino acids into the collagen backbone at precise
locations and optimize thermodynamic stability of the linear and cyclic peptides. The modular nature of
our new collagen peptide systems will provide highly tunable platforms into which any biologically
relevant protein binding sequence can be integrated. Our collagen peptide mimics will serve as new
chemical tools for understanding the fundamental biology and biochemistry of the collagen-protein
interactome. The proposed studies could ultimately serve as the fundamental science leading to future
biomedical treatments for pathologies in which precisely modulating collagen-protein interactions could
significantly enhance patient outcome.

## Key facts

- **NIH application ID:** 10399415
- **Project number:** 5R01AR077094-02
- **Recipient organization:** UNIVERSITY OF PENNSYLVANIA
- **Principal Investigator:** David Michael Chenoweth
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2022
- **Award amount:** $494,602
- **Award type:** 5
- **Project period:** 2021-05-01 → 2026-02-28

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10399415

## Citation

> US National Institutes of Health, RePORTER application 10399415, Peptide Mimics of the Collagen Triple Helix (5R01AR077094-02). Retrieved via AI Analytics 2026-05-23 from https://api.ai-analytics.org/grant/nih/10399415. Licensed CC0.

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