Synthetic antibody-derived immunopeptide provides neuroprotection in glaucoma through molecular interaction with retinal protein histone H3.1.

Glaucoma is a group of optic neuropathies characterized by the progressive degeneration of retinal ganglion cells (RGCs) as well as their axons leading to irreversible loss of sight. Medical management of the intraocular pressure (IOP) still represents the gold standard in glaucoma therapy, which only manages a single risk factor and does not directly address the neurodegenerative component of this eye disease. Recently, our group showed that antibody-derived immunopeptides (encoding complementarity-determining regions, CDRs) provide attractive glaucoma medication candidates and directly interfere its pathogenic mechanisms by different modes of action.

An account on the factors determining the extra stability of the -hairpin from B1 domain of protein G.

The folding-unfolding of a 16 residue polypeptide, a -hairpin in B1 domain of protein G is investigated here to account for the factors assisting the extra stability of the polypeptide in the presence of an explicit solvent and even when a denaturant like urea is present in the medium. It is observed here that the backbone H-bond network well defines the folded state and is even capable of forming the folded state, but it is not the only criteria for making a stable -hairpin fold. Factors such as the side chain H-bonds and the alignment of the certain hydrophobic group side chains play a prominent role in preserving the -hairpin structure and thus providing an extra stability to the hairpin architecture.