Membrane electrostatics sensed by tryptophan anchors in hydrophobic model peptides depends on non-aromatic interfacial amino acids: implications in hydrophobic mismatch

Abstract

WALPs are synthetic α-helical membrane-spanning peptides that constitute a well-studied system for exploring hydrophobic mismatch. These peptides represent a simplified consensus motif for transmembrane domains of intrinsic membrane proteins due...

Design, Synthesis and Activity of New N1-Alkyl Tryptophan Functionalized Dendrimeric Peptides against Glioblastoma

“…Design of the present Trp-rich peptide dendrimers with N 1 -atom substituted with N 1 -alkyl ( 19 – 21 ) or N 1 -alkylamino residue ( 24 – 25 ) ( Figure 2 ) was prompted by multiple functions played by Trp, e.g., structural stabilization of the spanning membrane peptides and proteins [ 32 , 33 , 34 ], antioxidant properties [ 53 , 54 ], and involvement of its catabolic products in development of immunosuppression in cancer disease [ 35 , 36 , 37 ]. According to the current knowledge, natural peptides express variability of anticancer mechanisms, including membrane disintegration and induction of apoptosis by reactive-oxygen-species accumulation.…”

“…Trp is an aromatic amino acid that is often found in hydrophobic tails of peptides or membrane proteins spanning lipid bilayers [ 32 ]. Due to its hydrophobic character and ability to be involved in hydrogen bonding, pi–cation, and other non-covalent interactions it is often located at water/lipid bilayer interface, where it plays a role of an anchor and protein structure stabilizer [ 33 , 34 ].…”

Hydration Dynamics in Biological Membranes: Emerging Applications of Terahertz Spectroscopy

“…Notably, work from our group (utilizing the wavelength-selective fluorescence approach 8,19 ) has established solvation dynamics of membrane interfacial tryptophan residues as a sensitive reporter for several biological phenomena including membrane lysis, 20 trans-membrane ion conductance, 21 and response to membrane hydrophobic mismatch. 22,23 Recent reports on the restricted dynamics and anomalous diffusion of water in the translocon protein machinery involved in in cellulo membrane insertion and folding of nascent membrane-spanning proteins 24 have further broadened the organizational repertoire of water in membrane biology. Viewer.…”

“…Aromatic amino acids (such as tryptophan, shown as yellow beads in Figure a) play an important role in this context because of their propensity for participating in hydrogen bonds with lipid carbonyl, phosphate and choline groups − and interacting with membrane interfacial water, which stabilizes initial peptide–membrane contacts. Notably, work from our group (utilizing the wavelength-selective fluorescence approach , ) has established solvation dynamics of membrane interfacial tryptophan residues as a sensitive reporter for several biological phenomena including membrane lysis, transmembrane ion conductance, and response to membrane hydrophobic mismatch. , Recent reports on the restricted dynamics and anomalous diffusion of water in the translocon protein machinery involved in in cellulo membrane insertion and folding of nascent membrane-spanning proteins have further broadened the organizational repertoire of water in membrane biology. The ubiquitous involvement of water in shaping the organization and dynamics of biological membranes is reflected in emerging reports on functionally relevant water molecules in almost every aspect of contemporary membrane biology.…”