Conformational control of integrin-subtype selectivity in isodgr peptide motifs: A biological switch

Andreas O. Frank; Elke Otto; Carlos Mas-Moruno; Herbert B. Schiller; Luciana Marinelli; Sandro Cosconati; Alexander Bochen; Dörte Vossmeyer; Grit Zahn; Roland Stragies; Ettore Novellino; Horst Kessler

doi:10.1002/anie.201004363

Conformational control of integrin-subtype selectivity in isodgr peptide motifs: A biological switch

Andreas O. Frank
, Elke Otto
, Carlos Mas-Moruno
, Herbert B. Schiller
, Luciana Marinelli
, Sandro Cosconati
, Alexander Bochen
, Dörte Vossmeyer
, Grit Zahn
, Roland Stragies
, Ettore Novellino
, Horst Kessler

TUM Emeriti of Excellence

Research output: Contribution to journal › Article › peer-review

69 Scopus citations

Abstract

The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to α5β 1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide.

Original language	English
Pages (from-to)	9278-9281
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	49
Issue number	48
DOIs	https://doi.org/10.1002/anie.201004363
State	Published - 22 Nov 2010

Keywords

NMR spectroscopy
cyclic pentapeptides
integrin ligands
isoDGR sequence
peptides

Access to Document

10.1002/anie.201004363

Cite this

Frank, A. O., Otto, E., Mas-Moruno, C., Schiller, H. B., Marinelli, L., Cosconati, S., Bochen, A., Vossmeyer, D., Zahn, G., Stragies, R., Novellino, E., & Kessler, H. (2010). Conformational control of integrin-subtype selectivity in isodgr peptide motifs: A biological switch. Angewandte Chemie - International Edition, 49(48), 9278-9281. https://doi.org/10.1002/anie.201004363

@article{53d11997b4aa4112b137c3c866d8b167,

title = "Conformational control of integrin-subtype selectivity in isodgr peptide motifs: A biological switch",

abstract = "The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to α5β 1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide.",

keywords = "NMR spectroscopy, cyclic pentapeptides, integrin ligands, isoDGR sequence, peptides",

author = "Frank, \{Andreas O.\} and Elke Otto and Carlos Mas-Moruno and Schiller, \{Herbert B.\} and Luciana Marinelli and Sandro Cosconati and Alexander Bochen and D{\"o}rte Vossmeyer and Grit Zahn and Roland Stragies and Ettore Novellino and Horst Kessler",

year = "2010",

month = nov,

day = "22",

doi = "10.1002/anie.201004363",

language = "English",

volume = "49",

pages = "9278--9281",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley and Sons Ltd",

number = "48",

}

Frank, AO, Otto, E, Mas-Moruno, C, Schiller, HB, Marinelli, L, Cosconati, S, Bochen, A, Vossmeyer, D, Zahn, G, Stragies, R, Novellino, E & Kessler, H 2010, 'Conformational control of integrin-subtype selectivity in isodgr peptide motifs: A biological switch', Angewandte Chemie - International Edition, vol. 49, no. 48, pp. 9278-9281. https://doi.org/10.1002/anie.201004363

TY - JOUR

T1 - Conformational control of integrin-subtype selectivity in isodgr peptide motifs

T2 - A biological switch

AU - Frank, Andreas O.

AU - Otto, Elke

AU - Mas-Moruno, Carlos

AU - Schiller, Herbert B.

AU - Marinelli, Luciana

AU - Cosconati, Sandro

AU - Bochen, Alexander

AU - Vossmeyer, Dörte

AU - Zahn, Grit

AU - Stragies, Roland

AU - Novellino, Ettore

AU - Kessler, Horst

PY - 2010/11/22

Y1 - 2010/11/22

N2 - The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to α5β 1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide.

AB - The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to α5β 1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide.

KW - NMR spectroscopy

KW - cyclic pentapeptides

KW - integrin ligands

KW - isoDGR sequence

KW - peptides

UR - https://www.scopus.com/pages/publications/78649529857

U2 - 10.1002/anie.201004363

DO - 10.1002/anie.201004363

M3 - Article

C2 - 20957712

AN - SCOPUS:78649529857

SN - 1433-7851

VL - 49

SP - 9278

EP - 9281

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 48

ER -

Conformational control of integrin-subtype selectivity in isodgr peptide motifs: A biological switch

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this