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Energetics of Vanilloid Activation of TRPV1 Ion Channel
Energetics of Vanilloid Activation of TRPV1 Ion Channel
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211151429
- ISBN
- 9798383608005
- DDC
- 612
- 저자명
- Li, Shisheng.
- 서명/저자
- Energetics of Vanilloid Activation of TRPV1 Ion Channel
- 발행사항
- [Sl] : University of California, Davis, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 107 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-02, Section: B.
- 주기사항
- Advisor: Zheng, Jie.
- 학위논문주기
- Thesis (Ph.D.)--University of California, Davis, 2024.
- 초록/해제
- 요약Ligand activation of the nociceptive TRPV1 ion channel by vanilloids is a proven and powerful pathway for pain management and serves as one of the best model systems for analyzing allosteric coupling in ion channels. However, vanilloid binding and activation have been mostly described only qualitatively in the past. We developed a novel method to isolate channel gating states with a specific number of bound ligands and bound configuration, which allowed direct measurement of binding affinity and gating energetics on a per subunit basis. We determined that capsaicin binds to a rat TRPV1 subunit with an association constant of 2.4X106 M-1 , and found ligand binding to each subunit is nearly independent. Each ligand binding contributes 1.70 to 1.86 kcal/mol activation energy. Subunit contributions are nearly equal as postulated in the MWC model, with a minor deviation that two capsaicin molecules bound to diagonal subunits yield stronger cooperativity (by 0.3 to 0.4 kcal/mol) than those bound to neighboring subunits.
- 일반주제명
- Physiology
- 일반주제명
- Biophysics
- 일반주제명
- Cellular biology
- 일반주제명
- Biochemistry
- 키워드
- Allostery
- 키워드
- Ligand gating
- 키워드
- TRPV1
- 키워드
- Vanilloids
- 기타저자
- University of California, Davis Molecular Cellular and Integrative Physiology
- 기본자료저록
- Dissertations Abstracts International. 86-02B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520250211151429
■006m o d
■007cr#unu||||||||
■020 ▼a9798383608005
■035 ▼a(MiAaPQ)AAI31295125
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a612
■1001 ▼aLi, Shisheng.
■24510▼aEnergetics of Vanilloid Activation of TRPV1 Ion Channel
■260 ▼a[Sl]▼bUniversity of California, Davis▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a107 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-02, Section: B.
■500 ▼aAdvisor: Zheng, Jie.
■5021 ▼aThesis (Ph.D.)--University of California, Davis, 2024.
■520 ▼aLigand activation of the nociceptive TRPV1 ion channel by vanilloids is a proven and powerful pathway for pain management and serves as one of the best model systems for analyzing allosteric coupling in ion channels. However, vanilloid binding and activation have been mostly described only qualitatively in the past. We developed a novel method to isolate channel gating states with a specific number of bound ligands and bound configuration, which allowed direct measurement of binding affinity and gating energetics on a per subunit basis. We determined that capsaicin binds to a rat TRPV1 subunit with an association constant of 2.4X106 M-1 , and found ligand binding to each subunit is nearly independent. Each ligand binding contributes 1.70 to 1.86 kcal/mol activation energy. Subunit contributions are nearly equal as postulated in the MWC model, with a minor deviation that two capsaicin molecules bound to diagonal subunits yield stronger cooperativity (by 0.3 to 0.4 kcal/mol) than those bound to neighboring subunits.
■590 ▼aSchool code: 0029.
■650 4▼aPhysiology
■650 4▼aBiophysics
■650 4▼aCellular biology
■650 4▼aBiochemistry
■653 ▼aAllostery
■653 ▼aIntermediate states
■653 ▼aLigand gating
■653 ▼aTRPV1
■653 ▼aVanilloids
■690 ▼a0719
■690 ▼a0786
■690 ▼a0379
■690 ▼a0487
■71020▼aUniversity of California, Davis▼bMolecular, Cellular and Integrative Physiology.
■7730 ▼tDissertations Abstracts International▼g86-02B.
■790 ▼a0029
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17161676▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
