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Locations and functional roles of AGEs within collagen fibrils

Identify the exact locations of advanced glycation end-product (AGE) modifications within type I collagen fibrils and determine, for each site, whether the AGE acts as a cross-link between neighboring tropocollagen molecules or as a non-cross-linking adduct.

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Background

AGEs arise via the Maillard reaction and can either form cross-links between tropocollagen molecules or attach without cross-linking. The specific sites and functional roles are poorly characterized within mineralized fibrils.

Modeling studies often assume random placement due to the lack of site-specific data, which limits validation and mechanistic interpretation of AGE-induced changes in fibril mechanics.

References

Aside from computational studies concentrating on individual AGEs (Collier et al., 2015; Gautieri et al., 2014), their exact location and where they act as cross-linking or non-cross-linking AGEs is unknown.

— Mineral and cross-linking in collagen fibrils: The mechanical behavior of bone tissue at the nano-scale (2403.11753 - Kamml et al., 18 Mar 2024) in Section 2.3 Insertion of AGEs cross-links, Page 3