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Arg‐Gly‐Asp constrained within cyclic pentapoptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1

Open access
Aumailley, Monique, Gurrath, Marion, Müller, Gerhard, Calvete, Juan, Timpl, Rupert, Kessler, Horst·1991·FEBS Letters

Abstract

Cyclic Arg‐Gly‐Asp‐Phe‐Val peptides with either D‐Phe or D‐Val residues were 20‐ to more than 100‐fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly‐Arg‐Gly‐Asp‐Ser. No or only little increase in inhibitory capacity was observed for fibronectin adhesion and for the binding or platelet receptor αIIbβ3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all‐trans conformation with a βII′ and γ turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.

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Metadata

Authors
Aumailley, M., Gurrath, M., Müller, G., Calvete, J., Timpl, R., & Kessler, H.
Venue
FEBS Letters
Publisher
Wiley
Published
1991-10-07
Volume
291
Issue
1
Pages
50-54
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2074012988
Cited by
551
References
0
FWCI
4.72
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Arg‐Gly‐Asp constrained within cyclic pentapoptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1. https://app.cochat.ai/papers/10.1016/0014-5793(91)81101-d
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Aumailley, M., Gurrath, M., Müller, G., Calvete, J., Timpl, R., & Kessler, H. (1991). Arg‐Gly‐Asp constrained within cyclic pentapoptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1. FEBS Letters. https://doi.org/10.1016/0014-5793(91)81101-d

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