@article {46291,
	title = {In vitro and in silico studies on membrane interactions of diverse Capsicum annuum flower gamma-thionin peptides},
	journal = {Proteins-Structure Function and Bioinformatics},
	year = {2019},
	month = {AUG},
	type = {Article; Early Access},
	abstract = {<p>Thionins are small, cysteine-rich peptides that play an important role in plant defense, primarily through their interactions with membranes. Eight novel gamma-thionin peptides (CanThio1-8) were isolated from the flower of Capsicum annuum. Sequence analysis revealed that the peptides cluster into three groups. A representative peptide from each group (CanThio1, 2, and 3) was used for experimental characterization. Interestingly, peptides were found to possess some cytotoxic activity against normal human embryonic kidney cell line but higher cytotoxicity against cancer cell line MCF-7. CanThio3 peptide was chosen as a representative peptide to study the molecular mechanism of action on membranes. Microsecond timescale atomistic simulations of CanThio3 were performed in the presence of a POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) lipid bilayer. Simulations revealed that CanThio3 interacts with the bilayer and causes lipid thinning in the vicinity. Nonpolar amino acids specific to the alpha-core region of CanThio3 along with nonpolar residues in the gamma-core region are seen to interact with the lipid tails. The differences in the amino acid sequence of CanThio peptides in these regions explain the variability in cytotoxic activities. In summary, our results demonstrate the membrane-mediated activity of a novel series of gamma-thionin peptides from C. annuum.</p>
},
	keywords = {Capsicum annuum, Cytotoxicity, gamma-thionin, MD simulations, Membrane},
	issn = {0887-3585},
	doi = {10.1002/prot.25791},
	author = {Nikte, Siddhanta and Gahankari, Apurva and Mulla, Javed and Sengupta, Durba and Joshi, Manali and Tamhane, Vaijayanti}
}
@inbook {47812,
	title = {Molecular determinants of GPCR pharmacogenetics: deconstructing the population variants in β2-adrenergic receptor},
	booktitle = {Advances in Protein Chemistry and Structural Biology},
	volume = {128},
	year = {2022},
	month = {JAN},
	pages = {361-396},
	type = {Article},
	abstract = {<p>G protein-coupled receptors (GPCRs) are membrane proteins that play a central role in cell signaling and constitute one of the largest classes of drug targets. The molecular mechanisms underlying GPCR function have been characterized by several experimental and computational methods and provide an understanding of their role in physiology and disease. Population variants arising from nsSNPs affect the native function of GPCRs and have been implicated in differential drug response. In this chapter, we provide an overview on GPCR structure and activation, with a special focus on the β2-adrenergic receptor (β2-AR). First, we discuss the current understanding of the structural and dynamic features of the wildtype receptor. Subsequently, the population variants identified in this receptor from clinical and large-scale genomic studies are described. We show how computational approaches such as bioinformatics tools and molecular dynamics simulations can be used to characterize the variant receptors in comparison to the wildtype receptor. In particular, we discuss three examples of clinically important variants and discuss how the structure and function of these variants differ from the wildtype receptor at a molecular level. Overall, the chapter provides an overview of structure and function of GPCR variants and is a step towards the study of inter-individual differences and personalized medicine.</p>
},
	isbn = {9780323988957},
	doi = {10.1016/bs.apcsb.2021.08.002},
	author = {Joshi, Manali and Nikte, Siddhanta and Sengupta, Durba}
}
