The structure of a membrane-embedded alpha-helical reference protein, the M13 major coat protein, is characterized under different conditions of hydrophobic mismatch using fluorescence resonance energy transfer in combination with high-throughput mutagenesis. We show that the structure is similar in both thin (14:1) and thick (20:1) phospholipid bilayers, indicating that the protein does not undergo large structural rearrangements in response to conditions of hydrophobic mismatch. We introduce a "helical fingerprint" analysis, showing that amino acid residues 1-9 are unstructured in both phospholipid bilayers. Our findings indicate the presence of pi-helical domains in the transmembrane segment of the protein; however, no evidence is found for a structural adaptation to the degree of hydrophobic mismatch. In light of current literature, and based on our data, we conclude that aggregation (at high protein concentration) and adjustment of the tilt angle and the lipid structure are the dominant responses to conditions of hydrophobic mismatch.
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http://dx.doi.org/10.1529/biophysj.107.112698 | DOI Listing |
Langmuir
January 2025
Department of Chemical and Environmental Engineering, University of Cincinnati, Cincinnati, Ohio 45220, United States.
Solvent toxicity limits -butanol fermentation titer, increasing the cost and energy consumption for subsequent separation processes and making biobased production more expensive and energy-intensive than petrochemical approaches. Amphiphilic solvents such as -butanol partition into the cell membrane of fermenting microorganisms, thinning the transverse structure, and eventually causing a loss of membrane potential and cell death. In this work, we demonstrate the deleterious effects of -butanol partitioning upon the lateral dimension of the membrane structure, called membrane domains or lipid rafts.
View Article and Find Full Text PDFSoft Matter
December 2024
Multidisciplinary Centre for Advanced Materials, Institute for Frontier Medical Technology, School of Chemistry and Chemical Engineering, Shanghai University of Engineering Science, 333 Longteng Rd., Shanghai 201620, P. R. China.
Anal Chem
December 2024
Key Laboratory of Luminescence Analysis and Molecular Sensing (Southwest University), Ministry of Education, College of Chemistry and Chemical Engineering, Southwest University, Chongqing 400715, P. R China.
Herein, the bovine serum albumin (BSA)-loaded tetrakis[4-(4'-cyanophenyl)phenyl]ethane nanoaggregates (NAs) (BSA@TBPE-(CN) NAs) as a novel electrochemiluminescence (ECL) emitter were first prepared, which exhibited superior ECL performance via the newly defined protein-induced ECL enhancement. Impressively, BSA not only restricted the intramolecular motions by its hydrophobic cavity to improve optical radiation for enhancing ECL efficiency but also promoted the electrochemical excitation of BSA@TBPE-(CN) NAs in which amino acid residues of BSA altered the surface states and narrowed the energy gap of BSA@TBPE-(CN) NAs for further boosting the ECL efficiency. Furthermore, the BSA@TBPE-(CN) NAs displayed a more dispersed state due to electrostatic repulsion caused by its considerable negative charges, which was conducive to reacting more fully with coreactants for improving ECL emission.
View Article and Find Full Text PDFFront Mol Biosci
November 2024
Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-CEA-CNRS, Grenoble, France.
The primary goal of our work is to provide structural insights into the influence of the hydrophobic lipid environment on the membrane proteins (MPs) structure and function. Our work will not cover the well-studied hydrophobic mismatch between the lipid bilayer and MPs. Instead, we will focus on the less-studied direct molecular interactions of lipids with the hydrophobic surfaces of MPs.
View Article and Find Full Text PDFBioeng Transl Med
September 2024
Successful nerve repair using bioadhesive hydrogels demands minimizing tissue-material interfacial mechanical mismatch to reduce immune responses and scar tissue formation. Furthermore, it is crucial to maintain the bioelectrical stimulation-mediated cell-signaling mechanism to overcome communication barriers within injured nerve tissues. Therefore, engineering bioadhesives for neural tissue regeneration necessitates the integration of electroconductive properties with tissue-like biomechanics.
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