Cell receptor screening for human papillomavirus invasion by using a polyoxometalate-peptide assembly as a probe.

The present study constructed a competitive recognition system using cell receptor screening for human papillomavirus (HPV) invasion by using the hybrid-assembly of polyoxometalates (POMs) and cationic peptides as a platform. The fine tuning both of the surface charge of POMs and peptide sequence were precisely performed to develop a luminescence switch of POMs, leading to the establishment of a ternary system to identify which types of glycosaminoglycans (GAGs) are potential cell receptors for HPV infection. In addition, the method was successfully applied to construct a hybrid-assembly with the recombined HPV 16 L1 pentamers from Escherichia coli and perform GAGs screening, which validated the system's potential for practical applications.

A two-step binding process of Eu-containing polyoxometalates to bovine serum albumin.

Polyoxometalates (POMs) represent a type of typical polyanionic nanoclusters that can be utilized as inorganic bioactive materials; however, the detailed interactions of them with many target biomolecules such as peptides and proteins were not well clarified due to the complexity of the binding process. In the present study, the binding-induced physiochemical phenomena of a highly charged Eu-containing polyoxometalate, K13[Eu(SiW9Mo2O39)2] (EuSiWMo), with a model protein, bovine serum albumin (BSA), was identified upon the examination of luminescence of both the components during the titration. The large emission enhancement and subsequent quenching of the EuSiWMo were found in close relation to the amount of added BSA.