Biology subjects

Adewole, A.

Publications and source records attributed to Adewole, A..

3 recordsLinked to original sources

bioRxiv2026

Surface-specific film assembly of a Vibrio cholerae adhesin peptide modulated by environmental salts

Underwater adhesion research increasingly draws on bioinspired systems to uncover the molecular mechanisms that enable strong interfacial binding in aqueous environments. The biofilm adhesin Bap1 from Vibrio cholerae contains a short peptide motif, SYWFFGWHTK (CP), which exhibits exceptional adhesive performance, surpassing mussel foot protein mfp5 under comparable conditions. Despite its promise, the roles of ionic environments and aggregation behavior in governing CP adhesion remain unclear. In this study, we investigate how ion identity influences CP aggregation, film formation, and interfacial properties. Using dynamic light scattering, we identify the formation of micron-scale assemblies of aggregated molecular clusters (AAMCs), with size distributions modulated by salt type. Quartz crystal microbalance with dissipation and liquid atomic force microscopy reveal that CP film formation is both surface- and ion-dependent. On gold substrates, AAMCs preferentially adsorb and collapse into rigid, smooth nanofilms, consistent with hydrophobic-driven compaction. In contrast, silicate surfaces inhibit such collapse, yielding distinct morphologies and interfacial energetics. These findings demonstrate that surface chemistry and ionic conditions jointly regulate peptide aggregation and adhesion. This work provides mechanistic insight into hydrophobic-rich peptide systems and informs the rational design of next-generation wet adhesives, with broader implications for biomaterials and peptide-based formulations. GRAPHICAL ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=129 SRC="FIGDIR/small/733527v2_ufig1.gif" ALT="Figure 1"> View larger version (39K): org.highwire.dtl.DTLVardef@1f3f3cborg.highwire.dtl.DTLVardef@10aae0corg.highwire.dtl.DTLVardef@289970org.highwire.dtl.DTLVardef@171b026_HPS_FORMAT_FIGEXP M_FIG C_FIG

biophysics↗

bioRxiv2025

Vibrio cholerae adhesin-derived peptide mediates strong pull-off forces in aqueous high ionic strength environments

In this letter, the pull-off forces of adsorbed films of four Bap1-inspired peptides in various solvents were investigated on negatively charged mica substrates using the surface forces apparatus (SFA), complemented with dynamic light scattering (DLS) for characterizing the aggregation behavior of peptides in solution. Bap1-inspired peptides consisted of the 57 amino acid wild-type sequence (WT); a scrambled version of the WT used to investigate the impact of the primary amino acid sequence in pull-off forces (Scr); a ten amino acid sequence rich in hydrophobic content (CP) of the WT sequence, and an eight amino acid sequence (Sh1) that corresponds to the pseudo-repeating sequence in the 57 AA. SFA results showed remarkable pull-off forces for CP, particularly in the presence of salts: measured pull-off forces were 26.0 {+/-} 7.0 mN/m for no dwell-time and up to 42.0 {+/-} 8.8 mN/m when surfaces were left in contact for 30 minutes. DLS observations indicate that salts favor large peptide aggregation for all constructs (Hz > 1 {micro}m), as compared to milliQ (Hz {approx} 100-500 nm) water and DMSO (Hz {approx} 100 nm), resulting in heterogeneous peptide film thicknesses. This letter concludes with a comparison to the pull-off forces of mussel foot protein-inspired peptides reported in the literature.

biophysics↗

bioRxiv2022

Influence of Diphenyl Diselenide on Thiol Redox Homeostasis and Electrogenic Membrane Transport in Rotenone-Induced Parkinsons Disease

The central role of oxidative stress in the etiology of Parkinsons disease defines a key therapeutic role for antioxidant compounds in the management of the disease. Redox-sensitive proteins such as the Na+/K+-ATPase have also been implicated as one of the targets of oxidative stress. The present study sought to investigate the role of diphenyl diselenide (DPDSe) in amelioration of disturbed redox homeostasis and modulation of enzyme activity caused by rotenone administration to Wistar albino rats. In determining the best route of rotenone administration, animals were grouped into four namely: control, oral, intraperitoneal (IP) and subcutanoeus (SC) and administered rotenone (3mg/kg) via oral, intraperitoneal (IP) and subcutaneous routes, with controls receiving the vehicle (2% DMSO + 98% normal saline (0.85%)). Having observed a more deleterious impact in the with he IP route, this mode of rotenone administration was selected along with oral administration of DPDSe (10mg/kg). this was done with four groups of animals namely: control, DPDSe, rotenone and DPDSe+rotenone. The effect of treatment was evaluated after seven days for total and non-protein thiol levels, lipid peroxidation and Na+/K+-ATPase activity. The result demonstrated the antioxidant potential of DPDSe in attenuating depletion of thiols, and lipid peroxidation caused by rotenone. It is apparent that DPDSe is a promising therapeutic agent in the management of PD, hence further investigations into its impact on different pathways is expedient in the search for an effective treatment for PD. HighlightsO_LIIntraperitoneal administration of rotenone gives a comparatively faster development of Parkinsons disease features in rodents C_LIO_LIRotenone mediates depletion of total and non-protein thiol levels in the pathogenesis of Parkinsons disease C_LIO_LIDiphenyl diselenide significantly attenuates thiol depletion and lipid peroxidation mediated by rotenone C_LIO_LIRotenone-mediated inactivation of Na+/K+-ATPase in Parkinsons disease etiology may involve ATP depletion C_LI

pharmacology and toxicology↗