Light-activated thiomaleimide crosslinking stabilizes collagen mimetic peptide triple helix

Rafael Castro; Shashika Gammanchiralage; Christopher Price; April Kloxin

doi:10.1039/d6cc01755j

January 1, 2026Chemical CommunicationsOpen Access

Light-activated thiomaleimide crosslinking stabilizes collagen mimetic peptide triple helix

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Key Points

This research aims to enhance the stability of collagen mimetic peptides using light-activated crosslinking methods.
Demonstrated rapid stabilization of collagen mimetic peptides via UV activation.
Utilized thiomaleimide crosslinking to form stable triple helices.
Conducted assessments of biomaterial structure and function.
Achieved significant stabilization of the triple helix structure under UV activation.
Showed improved performance metrics for the resulting biomaterials.

Implication

Demonstrates stabilization of collagen mimetic peptides, suggesting enhanced biomaterial properties.

Abstract

Collagen mimetic peptides (CMPs) are useful self-assembling building blocks for creating tunable biomaterials with structure and function dependent on triple helix stability. We demonstrate rapid, UV-activated stabilization of a CMP...

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Cite This Study

Castro et al. (2026) studied this question.

synapsesocial.com/papers/6a37808224f042ddf4c5aa24 https://doi.org/10.1039/d6cc01755j

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Light-activated thiomaleimide crosslinking stabilizes collagen mimetic peptide triple helix

Key Points

Implication

Abstract

Discussion

Cite This Study

Light-activated thiomaleimide crosslinking stabilizes collagen mimetic peptide triple helix

Key Points

Implication

Abstract

Discussion

Cite This Study

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