Improving synthesis and binding affinities of nucleic acid aptamers and their therapeutics and diagnostic applications
Biophys Chem. 2024 Mar 21;309:107218. doi: 10.1016/j.bpc.2024.107218. Online ahead of print.ABSTRACTNucleic acid aptamers have captivated the attention of analytical and medicinal scientists globally due to their several advantages as recognition molecules over conventional antibodies because of their small size, simple and inexpensive synthesis, broad target range, and high stability in varied environmental conditions. These recognition molecules can be chemically modified to make them resistant to nuclease action in blood serum, reduce rapid renel clearance, improve the target affinity and selectivity, and make them amen...
Source: Biophysical Chemistry - March 28, 2024 Category: Chemistry Authors: Malaya Mili Vinay Bachu Pooja Rani Kuri Naveen Kumar Singh Pranab Goswami Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 May;308:107217. doi: 10.1016/j.bpc.2024.107217. Epub 2024 Mar 11.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high temperature...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 May;308:107217. doi: 10.1016/j.bpc.2024.107217. Epub 2024 Mar 11.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high temperature...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 May;308:107217. doi: 10.1016/j.bpc.2024.107217. Epub 2024 Mar 11.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high temperature...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 May;308:107217. doi: 10.1016/j.bpc.2024.107217. Epub 2024 Mar 11.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high temperature...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 May;308:107217. doi: 10.1016/j.bpc.2024.107217. Epub 2024 Mar 11.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high temperature...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 Mar 11;308:107217. doi: 10.1016/j.bpc.2024.107217. Online ahead of print.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high tem...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 Mar 11;308:107217. doi: 10.1016/j.bpc.2024.107217. Online ahead of print.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high tem...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 Mar 11;308:107217. doi: 10.1016/j.bpc.2024.107217. Online ahead of print.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high tem...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 Mar 11;308:107217. doi: 10.1016/j.bpc.2024.107217. Online ahead of print.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high tem...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
H < sub > 2 < /sub > production under stress: [FeFe] ‑hydrogenases reveal strong stability in high pressure environments
Biophys Chem. 2024 Mar 11;308:107217. doi: 10.1016/j.bpc.2024.107217. Online ahead of print.ABSTRACTHydrogenases are a diverse group of metalloenzymes that catalyze the conversion of H2 into protons and electrons and the reverse reaction. A subgroup is formed by the [FeFe]‑hydrogenases, which are the most efficient enzymes of microbes for catalytic H2 conversion. We have determined the stability and activity of two [FeFe]‑hydrogenases under high temperature and pressure conditions employing FTIR spectroscopy and the high-pressure stopped-flow methodology in combination with fast UV/Vis detection. Our data show high tem...
Source: Biophysical Chemistry - March 15, 2024 Category: Chemistry Authors: Kristina Edenharter Michel W Jaworek Vera Engelbrecht Roland Winter Thomas Happe Source Type: research
Understanding the bio-crystallization: An insight to therapeutic relevance
Biophys Chem. 2024 Mar 5;308:107216. doi: 10.1016/j.bpc.2024.107216. Online ahead of print.ABSTRACTIn the realm of biomedical engineering and materials science, the synthesis of biomaterials plays a pivotal role in advancing therapeutic strategies for regeneration of tissues. The deliberate control of crystallization processes in biomaterial synthesis has emerged as a key avenue for tailoring the properties of these materials, enabling the design of innovative solutions for a wide array of medical applications. This review delves into the interplay between controlled crystallization and biomaterial synthesis, exploring its...
Source: Biophysical Chemistry - March 13, 2024 Category: Chemistry Authors: Vivek Pandey Tejasvi Pandey Source Type: research
Understanding the bio-crystallization: An insight to therapeutic relevance
Biophys Chem. 2024 Mar 5;308:107216. doi: 10.1016/j.bpc.2024.107216. Online ahead of print.ABSTRACTIn the realm of biomedical engineering and materials science, the synthesis of biomaterials plays a pivotal role in advancing therapeutic strategies for regeneration of tissues. The deliberate control of crystallization processes in biomaterial synthesis has emerged as a key avenue for tailoring the properties of these materials, enabling the design of innovative solutions for a wide array of medical applications. This review delves into the interplay between controlled crystallization and biomaterial synthesis, exploring its...
Source: Biophysical Chemistry - March 13, 2024 Category: Chemistry Authors: Vivek Pandey Tejasvi Pandey Source Type: research
Understanding the bio-crystallization: An insight to therapeutic relevance
Biophys Chem. 2024 Mar 5;308:107216. doi: 10.1016/j.bpc.2024.107216. Online ahead of print.ABSTRACTIn the realm of biomedical engineering and materials science, the synthesis of biomaterials plays a pivotal role in advancing therapeutic strategies for regeneration of tissues. The deliberate control of crystallization processes in biomaterial synthesis has emerged as a key avenue for tailoring the properties of these materials, enabling the design of innovative solutions for a wide array of medical applications. This review delves into the interplay between controlled crystallization and biomaterial synthesis, exploring its...
Source: Biophysical Chemistry - March 13, 2024 Category: Chemistry Authors: Vivek Pandey Tejasvi Pandey Source Type: research
The processing intermediate of human amylin, pro-amylin(1-48), has in vivo and in vitro bioactivity
Biophys Chem. 2024 Feb 15;308:107201. doi: 10.1016/j.bpc.2024.107201. Online ahead of print.ABSTRACTAmylin is released by pancreatic beta-cells in response to a meal and its major soluble mature form (37 amino acid-peptide) produces its biological effects by activating amylin receptors. Amylin is derived from larger propeptides that are processed within the synthesizing beta-cell. There are suggestions that a partially processed form, pro-amylin(1-48) is also secreted. We tested the hypothesis that pro-amylin(1-48) has biological activity and that human pro-amylin(1-48) may also form toxic pre-amyloid species. Amyloid form...
Source: Biophysical Chemistry - March 7, 2024 Category: Chemistry Authors: Giulia Mazzini Christelle Le Foll Christina N Boyle Michael L Garelja Alexander Zhyvoloup Matthew E T Miller Debbie L Hay Daniel P Raleigh Thomas A Lutz Source Type: research
