Understanding the Interactions of Guanine Quadruplexes with Peptides as Novel Strategies for Diagnosis or Tuning Biological Functions

Abstract

Guanine quadruplexes (G4s) are nucleic acid structures exhibiting a complex structural behavior and exerting crucial biological functions in both cells and viruses. The specific interactions of peptides with G4s, as well as an understanding of the factors driving the specific recognition are important for the rational design of both therapeutic and diagnostic agents. In this review, we examine the most important studies dealing with the interactions between G4s and peptides, highlighting the strengths and limitations of current analytic approaches. We also show how the combined use of high‐level molecular simulation techniques and experimental spectroscopy is the best avenue to design specifically tuned and selective peptides, thus leading to the control of important biological functions.

The anticancer peptide LL-III binds with nanomolar affinity to human telomeric and cMyc G-quadruplexes

“…Of note, LL-III is a natural and short peptide (15 amino acids) with a sequence that differs considerably from those of other peptides reported to bind to quadruplexes (Table S2, ESI †). 13,15,24,25 Further, it belongs to a class of peptides (AMPs and ACPs) whose ability to bind to G-quadruplexes is almost unexplored. For this reason, it may…”