Journal Article PUBDB-2020-04618

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Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules

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2020
Wiley-VCH Weinheim

Angewandte Chemie / International edition 59(14), 5747-5755 () [10.1002/anie.201914101]
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Abstract: Collagen model peptides (CMPs) serve as tools for understanding stability and function of the collagen triple helix and have a potential for biomedical applications. In the past, interstrand 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 were preorganized in a PPII‐helix‐type conformation by a functionalizable intrastrand C$_2$ 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.

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Contributing Institute(s):
  1. EMBL-User (EMBL-User)
Research Program(s):
  1. 6G3 - PETRA III (POF3-622) (POF3-622)
Experiment(s):
  1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2020
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Medline ; Creative Commons Attribution CC BY 4.0 ; OpenAccess ; Chemical Reactions ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 10 ; Index Chemicus ; JCR ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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 Record created 2020-11-26, last modified 2025-07-29


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