دورية أكاديمية

Synthetic Diversity and Catalytic Mechanism of Peptide Dendrimers

التفاصيل البيبلوغرافية
العنوان: Synthetic Diversity and Catalytic Mechanism of Peptide Dendrimers
المؤلفون: Estelle Delort, Tamis Darbre, Jean-Louis Reymond
المصدر: CHIMIA, Vol 59, Iss 3 (2005)
بيانات النشر: Swiss Chemical Society, 2005.
سنة النشر: 2005
المجموعة: LCC:Chemistry
مصطلحات موضوعية: Dendrimer, Enzyme model, Ester hydrolysis, Peptide, Solid-phase synthesis, Chemistry, QD1-999
الوصف: Peptide dendrimers composed of alternating sequences of natural amino acids and branching diamino acids are investigated as synthetic enzyme models. The dendrimers can be prepared by solid-phase peptide synthesis and are obtained pure in yields of 5–35%. Peptide dendrimers with surface histidine residues catalyze ester hydrolysis reaction with enzyme-like kinetics, including substrate binding (KM), catalytic turnover (kcat), and rate acceleration kcat/kuncat = 1000–20'000. Mechanistic investigation by substrate variation, pH-profile, and isothermaltitration calorimetry show that the catalytic effect is caused by positive interaction between the histidine side-chains and creation of a hydrophobic microenvironment for substrate binding.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: German
English
French
تدمد: 0009-4293
2673-2424
Relation: https://chimia.ch/chimia/article/view/3950; https://doaj.org/toc/0009-4293; https://doaj.org/toc/2673-2424
DOI: 10.2533/000942905777676768
URL الوصول: https://doaj.org/article/8f8da34cfd32412c9c27b0a298961b4f
رقم الأكسشن: edsdoj.8f8da34cfd32412c9c27b0a298961b4f
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:00094293
26732424
DOI:10.2533/000942905777676768