✦ LIBER ✦

Molecular interaction analysis in ligand design using mass transport, kinetic and thermodynamic methods

✍ Scribed by Michael L. Doyle; David G. Myszka; Irwin M. Chaiken

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 833 KB
Volume: 9
Category: Article
ISSN: 0952-3499
DOI: 10.1002/(sici)1099-1352(199603)9:2<65::aid-jmr245>3.0.co;2-b

No coin nor oath required. For personal study only.

✦ Synopsis

Ligand design in biotechnology is underpinned by the control of molecular affinity. Hence, measuring binding interactions is a key component in designing ligands for such uses as therapeutics, diagnostics, biomaterials and separation science. Mass transport, kinetic and thermodynamic methods have been used for macromolecular interaction analysis but also have potential applicability as direct methods for measuring small molecular interactions. They can enhance the ligand design process by providing the ability to choose ligands based on both their kinetic and thermodynamic binding properties.

📜 SIMILAR VOLUMES

Real-Time Competitive Kinetic Analysis o

Real-Time Competitive Kinetic Analysis of Interactions between Low-Molecular-Weight Ligands in Solution and Surface-Immobilized Receptors

✍ R. Karlsson 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 801 KB

With surface plasmon resonance detection it is possible to measure the binding kinetics between a macromolecule in solution and a receptor immobilized on a sensor surface. The detector response is proportional to the mass of the analyte that binds to the surface, and therefore, a direct observation

Design and use of multi-affinity surface

Design and use of multi-affinity surfaces in biomolecular interaction analysis–mass spectrometry (BIA/MS): a step toward the design of SPR/MS arrays

✍ Dobrin Nedelkov; Randall W. Nelson 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 154 KB

## Abstract The feasibility of multi‐affinity ligand surfaces in biomolecular interaction analysis–mass spectrometry (BIA/MS) was explored in this work. Multi‐protein affinity surfaces were constructed by utilizing antibodies to beta‐2‐microglobulin, cystatin C, retinol binding protein, transthyret

Protein–Ligand Interactions. From Molecu

Protein–Ligand Interactions. From Molecular Recognition to Drug Design. (Vol. 19 of “Methods and Principles in Medicinal Chemistry”, Eds.: R. Mannhold, H. Kubinyi, and G. Folkers). By Hans-Joachim Böhm and Gisbert Schneider.

✍ Gerhard Hessler 📂 Article 📅 2004 🏛 John Wiley and Sons 🌐 English ⚖ 63 KB 👁 2 views

Protein and peptide analysis by mass spe

Protein and peptide analysis by mass spectrometry J. R. Chapman (Ed.), Methods in Molecular Biology, Vol. 61, The Humana Press, Totowa, NJ, USA 1996, pp. 1–352, ISBN 0-89603-345-7, US $ 69.50

✍ Friedrich Lottspeich 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 77 KB