Complexity of αvβ6-integrin targeting RGD peptide trimers: emergence of non-specific binding by synergistic interaction-Reference-Cited by-同舟云学术

Complexity of αvβ6-integrin targeting RGD peptide trimers: emergence of non-specific binding by synergistic interaction

Published:2023 Issue:12 Volume:14 Page:2564-2573
ISSN:2632-8682
Container-title:RSC Medicinal Chemistry
language:en
Short-container-title:RSC Med. Chem.

Author:

Quigley Neil Gerard¹,Richter Frauke¹,Kossatz Susanne²,Notni Johannes¹³^ORCID

Affiliation:

1. Institute of Pathology, School of Medicine, Technische Universität München, Trogerstr. 18, D-81675 München, Germany

2. Department of Nuclear Medicine, University Hospital Klinikum Rechts der Isar and Central Institute for Translational Cancer Research, (TranslaTUM), School of Medicine, Technische Universität München, Munich, Germany

3. TRIMT GmbH, Carl-Eschebach-Str. 7, D-01454 Radeberg, Germany

Abstract

A single O atom at the right position halves liver uptake of αvβ6-integrin targeting RGD peptide trimers. As there is no correlation with polarity proxies, this is interpreted as an emergent phenomenon arising from loss of synergistic interaction.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Drug Discovery,Pharmaceutical Science,Pharmacology,Molecular Medicine,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/MD/D3MD00365E

Reference43 articles.

1. Designing Multivalent Ligands to Control Biological Interactions: From Vaccines and Cellular Effectors to Targeted Drug Delivery

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