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Search Publications by: Vitalii Silin (Assoc)

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Displaying 1 - 25 of 64

Copper-binding anticancer peptides from the piscidin family: an expanded mechanism that encompasses physical and chemical bilayer disruption

June 16, 2021
Author(s)
Fatih Comert, Frank N. Heinrich, Ananda Chowdhury, Mason Schoeneck, Caitlin Darling, Kyle Anderson, M. Daben J. Libardo, Alfredo Angeles-Boza, Vitalii I. Silin, Myriam Cotten, Mihaela Mihailescu
In the search for novel broad‑spectrum therapeutics to fight chronic infections, inflammation, and cancer, host defense peptides (HDPs) have garnered increasing interest. Characterizing their biologically‑active conformations and minimum motifs for

Structure and Function in Antimicrobial Piscidins: Histidine Position, Directionality of Membrane Insertion, and pH-Dependent Permeabilization

May 30, 2019
Author(s)
Mihaela Mihailescu, Mirco Sorci, Jolita Seckute, Vitalii I. Silin, Janet Hammer, B. Scott Perrin, Jorge Hernandez, Nedzada Smajic, Akritee Shrestha, Kimberly Bogadardus, Alexander Greenwood, Riqiang Fu, Jack Blazyk, Richard W. Pastor, Linda Nicholson, Georges Belfort, Myriam Cotten
Piscidins are histidine-enriched antimicrobial peptides that interact with lipid bilayers as amphipathic alpha-helices. Their activity at acidic and basic pH in vivo makes them promising templates for biomedical applications. This study focuses on p1 and

The role of human monoacylglycerol lipase (hMAGL) binding pocket in breakup of unsaturated phospholipid membranes

November 1, 2017
Author(s)
Ioannis L. Karageorgos, Vitalii I. Silin, nikolai zvonok, John P. Marino, David Janero, Alexandros Makriyannis
Human monoacylglycerol lipase (hMAGL) plays a key role in homeostatic tuning of the endocannabinoid signaling system and supports aggressive tumorogenesis, making this enzyme a promising therapeutic target. hMAGL features a membrane-associated lid domain

Structural Features and Lipid Binding Domain of Tubulin on Biomimetic Mitochondrial Membranes

April 18, 2017
Author(s)
David Paul Hoogerheide, Sergei Y. Noskov, Daniel Jacobs, Lucie Bergdoll, Vitalii Ivanovich Silin, David L. Worcester, Jeff Abramson, Hirsh Nanda, Tatiana K. Rostovtseva, Sergey M. Bezrukov
Amphitropic proteins, the subfamily of peripheral membrane proteins that interact directly with lipid bilayers, comprises members whose function depends on their localization either in the cytosol or at the cellular membranes. Despite the well-established

A Generalized Strategy for Immobilizing Uniformly Oriented Membrane Proteins at Solid Interfaces

February 13, 2013
Author(s)
Amit NMN Vaish, Vitalii I. Silin, Marlon L. Walker, Kristen L. Steffens, Susan Krueger, Alexei A. Yeliseev, Klaus Gawrisch, David J. Vanderah
We present here a generalized strategy for immobilizing uniformly oriented membrane proteins onto a functionalized surface. Using water soluble nitrilotriacetic acid (NTA)-terminated oligo(ethylene glycol) thiols, a histidine-tagged G protein-coupled

Surface Applications of Cavity Ring-Down Spectroscopy

October 16, 2008
Author(s)
A C. Pipino, Curtis Meuse, J P. Hoefnagels, Vitalii I. Silin, John T. Woodward IV
We report preliminary results describing two new applications of cavity ring-down spectroscopy (CRDS): 1) detection of non-absorbing species by refractive-index change using surface-plasmon-resonance (SPR)-enhanced CRDS, and 2) C-H overtone detection by