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Publication Abstract from PubMed

Collagen model peptides (CMPs) serve as tools for under-standing stability and function of the collagen triple helix and have a potential for biomedical applications. In the past, inter-strand cross-linking or conformational preconditioning of proline units through stereoelectronic effects have been utilized in the design of stabilized CMPs. To further study the effects determining collagen triple helix stability we investigated a series of CMPs containing synthetic diproline-mimicking modules (ProMs), which are preorganized in a PPII helix-type conformation by a functionalizable intra-strand C2-bridge. Results of CD-based denaturation studies were correlated with calculated (DFT) conformational preferences of the ProM units revealing that the relative helix stability is mainly governed by an interplay of main chain preorganization, ring flip preference, adaptability and steric effects. Triple helix integrity was proven by crystal structure analysis and binding to HSP47.

Triple Helix Stabilizing Effects in Collagen Model Peptides Containing PPII Helix-Preorganized Diproline Modules.,Schmalz HG, Maassen A, Gebauer J, Abraham ET, Grimm I, Neudorfl JM, Neundorf I, Baumann U Angew Chem Int Ed Engl. 2020 Jan 16. doi: 10.1002/anie.201914101. PMID:31944532^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.