biostudies-literatureUnknown13Alharbi SZeocin-binding protein (ZBP) confers resistance to the bleomycin family of antibiotics across a wide variety of prokaryotic and eukaryotic hosts. Zeocin is a bleomycin derivative used in cancer treatment. ZBP's mechanism involves binding to Zeocin, shielding DNA from damage. In protein folding studies, ZBP, a versatile marker across various organisms, can be used to track protein folding by fusing it to target proteins in prokaryotes and eukaryotes. Despite its significance, ZBP's biophysical properties are poorly studied. This study characterized the conformational changes, pH stability, solubility, and thermodynamic stability of recombinant ZBP from <i>Streptoalloteichus hindustanus</i>. ZBP's aggregation tendency was assessed across pH ranges, showing notable changes near its isoelectriFrontiers in molecular biosciences1748036https://www.ebi.ac.uk/biostudies/studies/S-EPMC12893952biostudies-literatureBiophysical insights into recombinant Zeocin binding protein: conformational stability and folding dynamics across pH and temperature.PMC12893952Malik AAlhomida AAlamri AAhmad TKhan MSAlharbi SKhan JMfalseBiophysical insights into recombinant Zeocin binding protein: conformational stability and folding dynamics across pH and temperature.Zeocin-binding protein (ZBP) confers resistance to the bleomycin family of antibiotics across a wide variety of prokaryotic and eukaryotic hosts. Zeocin is a bleomycin derivative used in cancer treatment. ZBP's mechanism involves binding to Zeocin, shielding DNA from damage. In protein folding studies, ZBP, a versatile marker across various organisms, can be used to track protein folding by fusing it to target proteins in prokaryotes and eukaryotes. Despite its significance, ZBP's biophysical properties are poorly studied. This study characterized the conformational changes, pH stability, solubility, and thermodynamic stability of recombinant ZBP from <i>Streptoalloteichus hindustanus</i>. ZBP's aggregation tendency was assessed across pH ranges, showing notable changes near its isoelectri2026-01-01T00:00:00Z20262026-07-07T03:09:51.276Z2026-07-07T03:08:23.898ZS-EPMC128939524169658010.3389/fmolb.2026.1748036