Synthetic Covalently Linked Dimeric Form of H2 Relaxin Retains Native RXFP1 Activity and Has Improved In Vitro Serum Stability
المؤلفون المشاركون
Separovic, Frances
Wade, John D.
Nair, Vinojini B.
Bathgate, Ross A. D.
Samuel, Chrishan S.
Hossain, Mohammed Akhter
المصدر
العدد
المجلد 2015، العدد 2015 (31 ديسمبر/كانون الأول 2015)، ص ص. 1-9، 9ص.
الناشر
Hindawi Publishing Corporation
تاريخ النشر
2015-01-22
دولة النشر
مصر
عدد الصفحات
9
التخصصات الرئيسية
الملخص EN
Human (H2) relaxin is a two-chain peptide member of the insulin superfamily and possesses potent pleiotropic roles including regulation of connective tissue remodeling and systemic and renal vasodilation.
These effects are mediated through interaction with its cognate G-protein-coupled receptor, RXFP1.
H2 relaxin recently passed Phase III clinical trials for the treatment of congestive heart failure.
However, its in vivo half-life is short due to its susceptibility to proteolytic degradation and renal clearance.
To increase its residence time, a covalent dimer of H2 relaxin was designed and assembled through solid phase synthesis of the two chains, including a judiciously monoalkyne sited B-chain, followed by their combination through regioselective disulfide bond formation.
Use of a bisazido PEG7 linker and “click” chemistry afforded a dimeric H2 relaxin with its active site structurally unhindered.
The resulting peptide possessed a similar secondary structure to the native monomeric H2 relaxin and bound to and activated RXFP1 equally well.
It had fewer propensities to activate RXFP2, the receptor for the related insulin-like peptide 3.
In human serum, the dimer had a modestly increased half-life compared to the monomeric H2 relaxin suggesting that additional oligomerization may be a viable strategy for producing longer acting variants of H2 relaxin.
نمط استشهاد جمعية علماء النفس الأمريكية (APA)
Nair, Vinojini B.& Bathgate, Ross A. D.& Separovic, Frances& Samuel, Chrishan S.& Hossain, Mohammed Akhter& Wade, John D.. 2015. Synthetic Covalently Linked Dimeric Form of H2 Relaxin Retains Native RXFP1 Activity and Has Improved In Vitro Serum Stability. BioMed Research International،Vol. 2015, no. 2015, pp.1-9.
https://search.emarefa.net/detail/BIM-1056550
نمط استشهاد الجمعية الأمريكية للغات الحديثة (MLA)
Nair, Vinojini B.…[et al.]. Synthetic Covalently Linked Dimeric Form of H2 Relaxin Retains Native RXFP1 Activity and Has Improved In Vitro Serum Stability. BioMed Research International No. 2015 (2015), pp.1-9.
https://search.emarefa.net/detail/BIM-1056550
نمط استشهاد الجمعية الطبية الأمريكية (AMA)
Nair, Vinojini B.& Bathgate, Ross A. D.& Separovic, Frances& Samuel, Chrishan S.& Hossain, Mohammed Akhter& Wade, John D.. Synthetic Covalently Linked Dimeric Form of H2 Relaxin Retains Native RXFP1 Activity and Has Improved In Vitro Serum Stability. BioMed Research International. 2015. Vol. 2015, no. 2015, pp.1-9.
https://search.emarefa.net/detail/BIM-1056550
نوع البيانات
مقالات
لغة النص
الإنجليزية
الملاحظات
Includes bibliographical references
رقم السجل
BIM-1056550
قاعدة معامل التأثير والاستشهادات المرجعية العربي "ارسيف Arcif"
أضخم قاعدة بيانات عربية للاستشهادات المرجعية للمجلات العلمية المحكمة الصادرة في العالم العربي
تقوم هذه الخدمة بالتحقق من التشابه أو الانتحال في الأبحاث والمقالات العلمية والأطروحات الجامعية والكتب والأبحاث باللغة العربية، وتحديد درجة التشابه أو أصالة الأعمال البحثية وحماية ملكيتها الفكرية. تعرف اكثر