Abstract
In this narrative review, we comprehensively review the available information about the recognition, structure, and dynamics of antimicrobial peptides (AMPs). Their complex behaviors occur across a wide range of time scales and have been challenging to portray. Recent advances in nuclear magnetic resonance and molecular dynamics simulations have revealed the importance of the molecular plasticity of AMPs and their abilities to recognize targets. We also highlight experimental data obtained using nuclear magnetic resonance methodologies, showing that conformational selection is a major mechanism of target interaction in AMP families.
Highlights
The biological functions of proteins are coded in their structures, and dynamic and conformational changes are key events in all processes that involve protein recognition [1,2,3,4]
More than 2500 antimicrobial peptides (AMPs) have been deposited in the Antimicrobial Peptide Database, and they represent a diversity of activities against bacteria, yeasts, fungi, viruses, and cancer cells [12,13]
Residues Lys-29, Ser-30, and Lys-32 showed increased R2 values in the presence of GAGs compared to free HBD6 in solution. Another interesting feature of this defensin is that the picosecond to nanosecond dynamics observed in the first residues located in the α-helix in the free state were reduced in the GAG-bound form, indicating that the α-helix becomes more structured upon GAG binding
Summary
The biological functions of proteins are coded in their structures, and dynamic and conformational changes are key events in all processes that involve protein recognition [1,2,3,4]. By identifying and analyzing the regions of local flexibility and cooperative motion of the residues inside a protein, we argue that it is possible to determine which parts of the protein will lead the kinetics of biologically relevant processes These regions are typically characterized by highly conserved residues within a family of proteins with related biological functions and are involved in binding interactions [2,3,10]. This complex behavior occurs across a wide range of time scales and has been challenging to portray. We summarize the methods that can be used to reveal molecular mechanisms of interaction, beginning with structure determination using NMR and proceeding to a high-resolution view of the structures and dynamics of their complexes
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
