Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates
The rapid protease degradation of peptides is currently limiting their therapeutic utility. Here, the authors report functionalised thiocarbazate scaffolds as precursors of aza-amino acids that can be integrated in peptide sequences, extending their bioavailability, and demonstrate this on FSSE/P577...
| Main Authors: | , , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-34712-9 |
| _version_ | 1811207756221251584 |
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| author | Ahmad Altiti Mingzhu He Sonya VanPatten Kai Fan Cheng Umair Ahmed Pui Yan Chiu Ibrahim T. Mughrabi Bayan Al Jabari Ronald M. Burch Kirk R. Manogue Kevin J. Tracey Betty Diamond Christine N. Metz Huan Yang LaQueta K. Hudson Stavros Zanos Myoungsun Son Barbara Sherry Thomas R. Coleman Yousef Al-Abed |
| author_facet | Ahmad Altiti Mingzhu He Sonya VanPatten Kai Fan Cheng Umair Ahmed Pui Yan Chiu Ibrahim T. Mughrabi Bayan Al Jabari Ronald M. Burch Kirk R. Manogue Kevin J. Tracey Betty Diamond Christine N. Metz Huan Yang LaQueta K. Hudson Stavros Zanos Myoungsun Son Barbara Sherry Thomas R. Coleman Yousef Al-Abed |
| author_sort | Ahmad Altiti |
| collection | DOAJ |
| description | The rapid protease degradation of peptides is currently limiting their therapeutic utility. Here, the authors report functionalised thiocarbazate scaffolds as precursors of aza-amino acids that can be integrated in peptide sequences, extending their bioavailability, and demonstrate this on FSSE/P5779 and bradykinin. |
| first_indexed | 2024-04-12T04:09:54Z |
| format | Article |
| id | doaj.art-a48c24524daa4e5cb8838c0018607cb6 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-12T04:09:54Z |
| publishDate | 2022-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-a48c24524daa4e5cb8838c0018607cb62022-12-22T03:48:32ZengNature PortfolioNature Communications2041-17232022-11-0113111310.1038/s41467-022-34712-9Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidatesAhmad Altiti0Mingzhu He1Sonya VanPatten2Kai Fan Cheng3Umair Ahmed4Pui Yan Chiu5Ibrahim T. Mughrabi6Bayan Al Jabari7Ronald M. Burch8Kirk R. Manogue9Kevin J. Tracey10Betty Diamond11Christine N. Metz12Huan Yang13LaQueta K. Hudson14Stavros Zanos15Myoungsun Son16Barbara Sherry17Thomas R. Coleman18Yousef Al-Abed19Institute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Molecular Medicine, Feinstein Institutes for Medical ResearchInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthApplied Immunotherapeutics, IncCenter for Molecular Innovation, Feinstein Institutes for Medical ResearchInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Molecular Medicine, Feinstein Institutes for Medical ResearchInstitute of Molecular Medicine, Feinstein Institutes for Medical ResearchInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthDonald and Barbara Zucker School of Medicine at Hofstra/NorthwellInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthInstitute of Molecular Medicine, Feinstein Institutes for Medical ResearchInstitute of Molecular Medicine, Feinstein Institutes for Medical ResearchCenter for Molecular Innovation, Feinstein Institutes for Medical ResearchInstitute of Bioelectronic Medicine, Feinstein Institutes for Medical Research, Northwell HealthThe rapid protease degradation of peptides is currently limiting their therapeutic utility. Here, the authors report functionalised thiocarbazate scaffolds as precursors of aza-amino acids that can be integrated in peptide sequences, extending their bioavailability, and demonstrate this on FSSE/P5779 and bradykinin.https://doi.org/10.1038/s41467-022-34712-9 |
| spellingShingle | Ahmad Altiti Mingzhu He Sonya VanPatten Kai Fan Cheng Umair Ahmed Pui Yan Chiu Ibrahim T. Mughrabi Bayan Al Jabari Ronald M. Burch Kirk R. Manogue Kevin J. Tracey Betty Diamond Christine N. Metz Huan Yang LaQueta K. Hudson Stavros Zanos Myoungsun Son Barbara Sherry Thomas R. Coleman Yousef Al-Abed Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates Nature Communications |
| title | Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates |
| title_full | Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates |
| title_fullStr | Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates |
| title_full_unstemmed | Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates |
| title_short | Thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates |
| title_sort | thiocarbazate building blocks enable the construction of azapeptides for rapid development of therapeutic candidates |
| url | https://doi.org/10.1038/s41467-022-34712-9 |
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