{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84495"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84495","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Myoglobin Microsperes and Metalloporphyrin -Peptide Complexes","abstract":"Addition of disulfide bridges and ionic contacts. We have synthesized and characterized a new class of heme-peptide complexes using disulfide-linked tweezers and cyclic peptides. The binding affinities, helicities, and mechanism of binding of linear, tweezers, and cyclic peptides to [Fe III(coproporphyrin-I)]+ have been determined. We have incorporated disulfide bridges between amphiphilic peptides to make tweezers---and even cyclic-peptides that bind heme extremely strongly, roughly 5 x 106 times more strongly than histidine itself. CD studies show that the cyclic peptide heme complexes are completely a-helical. Paramagnetic NMR shows that the 15-mer peptides bind sequentially, with an observable mono-peptide, high-spin intermediate. In contrast, the cyclic peptide complexes ligate both imidazoles cooperatively to the heme, producing only a low spin complex. Electrochemical measurements of the E1/2 of the FeIII(coproporphyrin-I) complexes of these peptides are all a fairly low potentials, ranging from -215 to -252 mV vs. NHE at pH 7. Addition of salt contacts to the design, resulted in the production of a highly helical complex. This peptide, bound to a diamagnetic and water soluble CoIII(coproporphyrin-I), has a stability toward denaturation of 3 kcal/mole.","abstract_html":"Addition of disulfide bridges and ionic contacts. We have synthesized and characterized a new class of heme-peptide complexes using disulfide-linked tweezers and cyclic peptides. The binding affinities, helicities, and mechanism of binding of linear, tweezers, and cyclic peptides to [Fe III(coproporphyrin-I)]+ have been determined. We have incorporated disulfide bridges between amphiphilic peptides to make tweezers---and even cyclic-peptides that bind heme extremely strongly, roughly 5 x 106 times more strongly than histidine itself. CD studies show that the cyclic peptide heme complexes are completely a-helical. Paramagnetic NMR shows that the 15-mer peptides bind sequentially, with an observable mono-peptide, high-spin intermediate. In contrast, the cyclic peptide complexes ligate both imidazoles cooperatively to the heme, producing only a low spin complex. Electrochemical measurements of the E1/2 of the FeIII(coproporphyrin-I) complexes of these peptides are all a fairly low potentials, ranging from -215 to -252 mV vs. NHE at pH 7. Addition of salt contacts to the design, resulted in the production of a highly helical complex. This peptide, bound to a diamagnetic and water soluble CoIII(coproporphyrin-I), has a stability toward denaturation of 3 kcal/mole.","abstract_has_math":false,"creators":["Rosenblatt, Michael Maurice"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Kenneth S. Suslick"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:14:48Z","date_published":"2015-09-25T22:14:48Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Chemistry, Analytical"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9990126"],"render_values":[{"text":"(MiAaPQ)AAI9990126","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84495","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kenneth S. 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We have synthesized and characterized a new class of heme-peptide complexes using disulfide-linked tweezers and cyclic peptides. The binding affinities, helicities, and mechanism of binding of linear, tweezers, and cyclic peptides to [Fe III(coproporphyrin-I)]+ have been determined. We have incorporated disulfide bridges between amphiphilic peptides to make tweezers---and even cyclic-peptides that bind heme extremely strongly, roughly 5 x 106 times more strongly than histidine itself. CD studies show that the cyclic peptide heme complexes are completely a-helical. Paramagnetic NMR shows that the 15-mer peptides bind sequentially, with an observable mono-peptide, high-spin intermediate. In contrast, the cyclic peptide complexes ligate both imidazoles cooperatively to the heme, producing only a low spin complex. Electrochemical measurements of the E1/2 of the FeIII(coproporphyrin-I) complexes of these peptides are all a fairly low potentials, ranging from -215 to -252 mV vs. NHE at pH 7. Addition of salt contacts to the design, resulted in the production of a highly helical complex. This peptide, bound to a diamagnetic and water soluble CoIII(coproporphyrin-I), has a stability toward denaturation of 3 kcal/mole.","Made available in DSpace on 2015-09-25T22:14:48Z (GMT). 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We have synthesized and characterized a new class of heme-peptide complexes using disulfide-linked tweezers and cyclic peptides. The binding affinities, helicities, and mechanism of binding of linear, tweezers, and cyclic peptides to [Fe III(coproporphyrin-I)]+ have been determined. We have incorporated disulfide bridges between amphiphilic peptides to make tweezers---and even cyclic-peptides that bind heme extremely strongly, roughly 5 x 106 times more strongly than histidine itself. CD studies show that the cyclic peptide heme complexes are completely a-helical. Paramagnetic NMR shows that the 15-mer peptides bind sequentially, with an observable mono-peptide, high-spin intermediate. In contrast, the cyclic peptide complexes ligate both imidazoles cooperatively to the heme, producing only a low spin complex. Electrochemical measurements of the E1/2 of the FeIII(coproporphyrin-I) complexes of these peptides are all a fairly low potentials, ranging from -215 to -252 mV vs. NHE at pH 7. Addition of salt contacts to the design, resulted in the production of a highly helical complex. This peptide, bound to a diamagnetic and water soluble CoIII(coproporphyrin-I), has a stability toward denaturation of 3 kcal/mole.","Made available in DSpace on 2015-09-25T22:14:48Z (GMT). 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