ArticleInternational journal of molecular sciences2015
Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Network Topology and Interactomic Analysis Reveal the Regulatory Framework of the Humanin Protein Family (MTRNR2Lx Class).Biomolecules · 2026Article
- The Ability of Chlorophyll to Trap Carcinogen Aflatoxin BInternational journal of molecular sciences · 2022Article
- Peptide-Based Drug-Delivery Systems in Biotechnological Applications: Recent Advances and Perspectives.Molecules (Basel, Switzerland) · 2019Review
- Retro-inverso Urokinase Receptor Antagonists for the Treatment of Metastatic Sarcomas.Scientific reports · 2017Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This work reports on the design and the synthesis of two short linear peptides both containing a few amino acids with disorder propensity and an allylic ester group at the C-terminal end. Their structural properties were firstly analyzed by means of experimental techniques in solution such as CD and NMR methods that highlighted peptide flexibility. These results were further confirmed by MD simulations that demonstrated the ability of the peptides to assume conformational ensembles. They revealed a network of transient and dynamic H-bonds and interactions with water molecules. Binding assays with a well-known drug-target, i.e., the CXCR4 receptor, were also carried out in an attempt to verify their biological function and the possibility to use the assays to develop new specific targets for CXCR4. Moreover, our data indicate that these peptides represent useful tools for molecular recognition processes in which a flexible conformation is required in order to obtain an interaction with a specific target.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.