Transglutaminase 2 has higher affinity for relaxed than for stretched fibronectin fibers.

Transglutaminase 2 (TG2) plays a vital role in stabilizing extracellular matrix (ECM) proteins through enzymatic crosslinking during tissue growth, repair, and inflammation. TG2 also binds non-covalently to fibronectin (FN), an essential component of the ECM, facilitating cell adhesion, migration, proliferation, and survival. However, the interaction between TG2 and fibrillar FN remains poorly understood, as most studies have focused on soluble or surface-adsorbed FN or FN fragments, which differ in their conformations from insoluble FN fibers.

Molecular dynamics of JUNO-IZUMO1 complexation suggests biologically relevant mechanisms in fertilization.

JUNO-IZUMO1 binding is the first known physical link created between the sperm and egg membranes in fertilization, however, how this initiates sperm-egg fusion remains elusive. As advanced structural insights will help to combat the infertility crisis, or advance fertility control, we employed all-atom Molecular Dynamics (MD) to derive dynamic structural insights that are difficult to obtain experimentally. We found that the hydrated JUNO-IZUMO1 interface is composed of a large set of short-lived non-covalent interactions.

A Linear Interaction Energy Model for Cavitand Host-Guest Binding Affinities.

Host-guest systems provide excellent models to explore molecular recognition in solution along with relevant technological applications from drug carriers to chemosensors. Here, we present a linear interaction energy (LIE) model to predict the binding affinity in host-guests with remarkable efficiency and predictive power. Using four host families, including cucurbiturils, octa acids, and β-cyclodextrin, and a large set (49) of chemically diverse guests, we demonstrate that binding-affinity predictions with a root mean square error <1.