Antimicrobial Peptides (AMPs), within their realm incorporate a diverse group of structurally
and functionally varied peptides, playing crucial roles in innate immunity. Over the last few decades,
the field of AMP has seen a huge upsurge, mainly owing to the generation of the so-called drug
resistant ‘superbugs’ as well as limitations associated with the existing antimicrobial agents. Due to
their resilient biological properties, AMPs can very well form the sustainable alternative for nextgeneration
therapeutic agents. Certain drawbacks associated with existing AMPs are, however, issues
of major concern, circumventing which are imperative. These limitations mainly include proteolytic
cleavage and hence poor stability inside the biological systems, reduced activity due to inadequate interaction
with the microbial membrane, and ineffectiveness because of inappropriate delivery among
others. In this context, the application of naturally occurring AMPs as an efficient prototype for generating
various synthetic and designed counterparts has evolved as a new avenue in peptide-based therapy.
Such designing approaches help to overcome the drawbacks of the parent AMPs while retaining
the inherent activity. In this review, we summarize some of the basic NMR structure based approaches
and techniques which aid in improving the activity of AMPs, using the example of a 16-residue dengue
virus fusion protein derived peptide, VG16KRKP. Using first principle based designing technique and
high resolution NMR-based structure characterization we validate different types of modifications of
VG16KRKP, highlighting key motifs, which optimize its activity. The approaches and designing techniques
presented can support our peers in their drug development work.
Crystal structure, characterization, Hirshfeld surface analysis and DFT studies of two [propane 3-bromo-1-(triphenyl phosphonium)] cations containing bromide (I) and tribromide (II) anions: The anion (II) as a new brominating agent for unsaturated compounds
