Multivalency as a Chemical Organization and Action Principle

Multivalent interactions can be applied universally for a targeted strengthening of an interaction between different interfaces or molecules. The binding partners form cooperative, multiple receptor–ligand interactions that are based on individually weak, noncovalent bonds and are thus generally reversible. Hence, multi‐ and polyvalent interactions play a decisive role in biological systems for recognition, adhesion, and signal processes. The scientific and practical realization of this principle will be demonstrated by the development of simple artificial and theoretical models, from natural systems to functional, application‐oriented systems. In a systematic review of scaffold architectures, the underlying effects and control options will be demonstrated, and suggestions will be given for designing effective multivalent binding systems, as well as for polyvalent therapeutics.     

A conformal mapping algorithm for the Bernoulli free boundary value problem

We propose a new numerical method for the solution of the Bernoulli free boundary value problem for harmonic functions in a doubly connected domain D in where an unknown free boundary Γ₀ is determined by prescribed Cauchy data on Γ₀ in addition to a Dirichlet condition on the known boundary Γ₁. Our main idea is to involve the conformal mapping method as proposed and analyzed by Akduman, Haddar, and Kress for the solution of a related inverse boundary value problem. For this, we interpret the free boundary Γ₀ as the unknown boundary in the inverse problem to construct Γ₀ from the Dirichlet condition on Γ₀ and Cauchy data on the known boundary Γ₁. Our method for the Bernoulli problem iterates on the missing normal derivative on Γ₁ by alternating between the application of the conformal mapping method for the inverse problem and solving a mixed Dirichlet–Neumann boundary value problem in D. We present the mathematical foundations of our algorithm and prove a convergence result. Some numerical examples will serve as proof of concept of our approach. Copyright © 2015 John Wiley & Sons, Ltd.     

Simultaneous serum desalting and total protein determination by macroporous reversed-phase chromatography

Macroporous reversed-phase (mRP) chromatography was successfully used to develop an accurate and precise method for total protein in serum. The limits of detection (0.83 μg, LOD) and quantification (2.51 μg, LOQ) for the mRP method are comparable with those of the widely used micro BCA protein assay. The mRP method can be used to determine the total protein concentration across a wide dynamic range by detecting chromatographic peaks at 215 nm and 280 nm. The method has the added advantage of desalting and denaturing proteins, leading to more complete digestion by trypsin and to better LC–MS–MS identification in shotgun proteomics experiments.