{"id":{"repo_id":"houston","oai_identifier":"oai:uh-ir.tdl.org:10657/17650"},"canonical_url":"https://search.dev.ndltd.org/etd/houston/oai:uh-ir.tdl.org:10657/17650","repository":{"repo_id":"houston","name":"University of Houston","base_url":"https://uh-ir.tdl.org/server/oai/request"},"display":{"title":"Bioactive Peptides as Antibacterial Agents and Visual Transduction","abstract":"Bioactive peptides (BPs) are specific protein fragments which positively impact bodily functions and primary health conditions. BPs are formed from amino acids linked by amide bonds and classified by their mode of action in health-related applications. The amino acid composition and their secondary structure determines their activity. More specifically, antimicrobial peptides (AMPs) are used in the development of novel antibacterial agents. The short killing time of the host pathogen with the use of BPs makes it difficult for pathogens to develop resistance in the cells. C18 is an AMP belonging to the cecropin family which I modified for evaluation as a potential therapeutic agent to treat severe methicillin resistant S. aureus (MRSA) infections via reverse sequencing and peptide stapling to enhance its compacity to penetrate lipid interfaces, improve helicity, and metabolic stability. Preliminary results support that these new BPs are antibacterial agents for further development to treat severe MRSA infections. The chemistry and biological assay results of synthesized peptides submitted for evaluation will be discussed in greater detail. Secondly, peripherin 2 (PRPH2) is a photoreceptor specific glycoprotein essential for proper formation of the rod and cone photoreceptor outer segments of the retina, which are the organelles responsible for visual transduction. Defective or absent PRPH2 protein results in various blinding retina diseases such as macular degeneration and retinitis pigmentosa (RP), which range in severity and time of onset. There is currently no known treatment for PRPH2 associated diseases. Therefore, the aim of this second peptide synthesis project is to ultimately develop a shorter drug lead for PRPH2 specific to a conserved region within the C-terminal domain. This region is flexible, functions as a signal sequence for localizing PRPH2 protein to the rod outer segment, critical in membrane fusion, disc morphogenesis, and disc shedding. Truncation and sequence reversal was performed to create thirteen new sequences that may penetrate lipid interfaces more efficiently or possibly function as a cleaved peptide while retaining its function as a shorter drug lead for further drug development for visual transduction. The chemistry and bioassay results for the synthesized peptides will be evaluated as this project is ongoing.","abstract_html":"Bioactive peptides (BPs) are specific protein fragments which positively impact bodily functions and primary health conditions. BPs are formed from amino acids linked by amide bonds and classified by their mode of action in health-related applications. The amino acid composition and their secondary structure determines their activity. More specifically, antimicrobial peptides (AMPs) are used in the development of novel antibacterial agents. The short killing time of the host pathogen with the use of BPs makes it difficult for pathogens to develop resistance in the cells. C18 is an AMP belonging to the cecropin family which I modified for evaluation as a potential therapeutic agent to treat severe methicillin resistant S. aureus (MRSA) infections via reverse sequencing and peptide stapling to enhance its compacity to penetrate lipid interfaces, improve helicity, and metabolic stability. Preliminary results support that these new BPs are antibacterial agents for further development to treat severe MRSA infections. The chemistry and biological assay results of synthesized peptides submitted for evaluation will be discussed in greater detail. Secondly, peripherin 2 (PRPH2) is a photoreceptor specific glycoprotein essential for proper formation of the rod and cone photoreceptor outer segments of the retina, which are the organelles responsible for visual transduction. Defective or absent PRPH2 protein results in various blinding retina diseases such as macular degeneration and retinitis pigmentosa (RP), which range in severity and time of onset. There is currently no known treatment for PRPH2 associated diseases. Therefore, the aim of this second peptide synthesis project is to ultimately develop a shorter drug lead for PRPH2 specific to a conserved region within the C-terminal domain. This region is flexible, functions as a signal sequence for localizing PRPH2 protein to the rod outer segment, critical in membrane fusion, disc morphogenesis, and disc shedding. Truncation and sequence reversal was performed to create thirteen new sequences that may penetrate lipid interfaces more efficiently or possibly function as a cleaved peptide while retaining its function as a shorter drug lead for further drug development for visual transduction. The chemistry and bioassay results for the synthesized peptides will be evaluated as this project is ongoing.","abstract_has_math":false,"creators":["Carty, Symone Louise"],"institution":"University of Houston","degree_name":"Doctor of Philosophy","degree_level":"Doctoral","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":["Gilbertson, Scott"],"committee_chairs":[],"committee_members":["May, Jeremy","Cai, Chengzhi","Zastrow, Melissa","Das, Joydip"],"year":2024,"date_issued":"2024-04-24","date_published":"2024-04-24","updated_at":"2026-07-24T02:32:58Z","subjects":["peptides, C18, microwave, reverse sequencing, ring closing metathesis, stapled antimicrobial peptides, RDS, PRPH2, photoreceptors, ROM-1"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/10657/17650","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Gilbertson, Scott"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["May, Jeremy","Cai, Chengzhi","Zastrow, Melissa","Das, Joydip"]},{"key":"dc:creator","label":"Author","values":["Carty, Symone Louise"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2024-07-26T03:44:03Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2024-07-26T03:44:03Z"]},{"key":"dc:date.issued","label":"Date","values":["2024-04-24"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Houston"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["peptides, C18, microwave, reverse sequencing, ring closing metathesis, stapled antimicrobial peptides, RDS, PRPH2, photoreceptors, ROM-1"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/10657/17650"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Bioactive peptides (BPs) are specific protein fragments which positively impact bodily functions and primary health conditions. BPs are formed from amino acids linked by amide bonds and classified by their mode of action in health-related applications. The amino acid composition and their secondary structure determines their activity. More specifically, antimicrobial peptides (AMPs) are used in the development of novel antibacterial agents. The short killing time of the host pathogen with the use of BPs makes it difficult for pathogens to develop resistance in the cells. C18 is an AMP belonging to the cecropin family which I modified for evaluation as a potential therapeutic agent to treat severe methicillin resistant S. aureus (MRSA) infections via reverse sequencing and peptide stapling to enhance its compacity to penetrate lipid interfaces, improve helicity, and metabolic stability. Preliminary results support that these new BPs are antibacterial agents for further development to treat severe MRSA infections. The chemistry and biological assay results of synthesized peptides submitted for evaluation will be discussed in greater detail. Secondly, peripherin 2 (PRPH2) is a photoreceptor specific glycoprotein essential for proper formation of the rod and cone photoreceptor outer segments of the retina, which are the organelles responsible for visual transduction. Defective or absent PRPH2 protein results in various blinding retina diseases such as macular degeneration and retinitis pigmentosa (RP), which range in severity and time of onset. There is currently no known treatment for PRPH2 associated diseases. Therefore, the aim of this second peptide synthesis project is to ultimately develop a shorter drug lead for PRPH2 specific to a conserved region within the C-terminal domain. This region is flexible, functions as a signal sequence for localizing PRPH2 protein to the rod outer segment, critical in membrane fusion, disc morphogenesis, and disc shedding. Truncation and sequence reversal was performed to create thirteen new sequences that may penetrate lipid interfaces more efficiently or possibly function as a cleaved peptide while retaining its function as a shorter drug lead for further drug development for visual transduction. The chemistry and bioassay results for the synthesized peptides will be evaluated as this project is ongoing."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Bioactive Peptides as Antibacterial Agents and Visual Transduction"]}]}],"canonical_facts":{"dc:contributor.advisor":["Gilbertson, Scott"],"dc:contributor.committeemember":["May, Jeremy","Cai, Chengzhi","Zastrow, Melissa","Das, Joydip"],"dc:creator":["Carty, Symone Louise"],"dc:date.accessioned":["2024-07-26T03:44:03Z"],"dc:date.available":["2024-07-26T03:44:03Z"],"dc:date.issued":["2024-04-24"],"dc:description.abstract":["Bioactive peptides (BPs) are specific protein fragments which positively impact bodily functions and primary health conditions. BPs are formed from amino acids linked by amide bonds and classified by their mode of action in health-related applications. The amino acid composition and their secondary structure determines their activity. More specifically, antimicrobial peptides (AMPs) are used in the development of novel antibacterial agents. The short killing time of the host pathogen with the use of BPs makes it difficult for pathogens to develop resistance in the cells. C18 is an AMP belonging to the cecropin family which I modified for evaluation as a potential therapeutic agent to treat severe methicillin resistant S. aureus (MRSA) infections via reverse sequencing and peptide stapling to enhance its compacity to penetrate lipid interfaces, improve helicity, and metabolic stability. Preliminary results support that these new BPs are antibacterial agents for further development to treat severe MRSA infections. The chemistry and biological assay results of synthesized peptides submitted for evaluation will be discussed in greater detail. Secondly, peripherin 2 (PRPH2) is a photoreceptor specific glycoprotein essential for proper formation of the rod and cone photoreceptor outer segments of the retina, which are the organelles responsible for visual transduction. Defective or absent PRPH2 protein results in various blinding retina diseases such as macular degeneration and retinitis pigmentosa (RP), which range in severity and time of onset. There is currently no known treatment for PRPH2 associated diseases. Therefore, the aim of this second peptide synthesis project is to ultimately develop a shorter drug lead for PRPH2 specific to a conserved region within the C-terminal domain. This region is flexible, functions as a signal sequence for localizing PRPH2 protein to the rod outer segment, critical in membrane fusion, disc morphogenesis, and disc shedding. Truncation and sequence reversal was performed to create thirteen new sequences that may penetrate lipid interfaces more efficiently or possibly function as a cleaved peptide while retaining its function as a shorter drug lead for further drug development for visual transduction. The chemistry and bioassay results for the synthesized peptides will be evaluated as this project is ongoing."],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["https://hdl.handle.net/10657/17650"],"dc:language.iso":["en"],"dc:subject":["peptides, C18, microwave, reverse sequencing, ring closing metathesis, stapled antimicrobial peptides, RDS, PRPH2, photoreceptors, ROM-1"],"dc:title":["Bioactive Peptides as Antibacterial Agents and Visual Transduction"],"dc:type":["Thesis"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Doctoral"],"thesis:degree_name":["Doctor of Philosophy"],"thesis:institution_name":["University of Houston"]},"updated_at":"2026-07-24T02:32:58Z"}