Electoral Violence, Partisan Identity, and Perceptions of Election Quality: A Survey Experiment in West Bengal, India

What are the consequences of election violence for citizens' political attitudes? We argue that in polarized contexts, citizens' interpretation of electoral violence depends on their partisan affiliations. When presented with information alleging co-partisans' involvement in violence, people with strong partisan identities become more likely to assert that elections were free and fair. We test this expectation with a vignette experiment in West Bengal after India's 2019 elections, presenting respondents with information about violence while varying the partisan identity of the perpetrator. Consistent with expectations, supporters of the Trinamool Congress (TMC) increased their evaluations of election quality when hearing about co-partisan violence. We find no evidence of disconfirmation bias for Bharatiya Janata Party (BJP) supporters; their recent shift to the party plausibly explains this finding.</p

Ligand Switching in Cell-Permeable Peptides: Manipulation of the α-Integrin Signature Motif

A synthetic cell-permeable peptide corresponding to the highly conserved α-integrin signature motif, Palmityl-K989VGFFKR995 (Pal-FF), induces integrin activation and aggregation in human platelets. Systematic replacement of the F992-F993 with amino acids of greater or lesser hydrophobicity to create Pal-KVGxxKR peptides demonstrate that hydrophobic amino acids (isoleucine, phenylalanine, tyrosine, tryptophan) are essential for agonist potency. In marked contrast, substitution with small and/or hydrophilic amino acids (glycine, alanine, serine) causes a switch in the biological activity resulting in inhibition of platelet aggregation, adhesion, ADP secretion, and thromboxane synthesis. These substituted, hydrophilic peptides are not true pharmacological antagonists, as they actively induce a phosphotyrosine signaling cascade in platelets. Singly substituted peptides (Pal-AF and Pal-FA) cause preferential retention of pro- or anti-thrombotic properties, respectively. Because the α-integrin signature motif is an established docking site for a number of diverse cytoplasmic proteins, we conclude that eliminating critical protein−protein interactions mediated through the hydrophobic amino acids, especially F993, favors an anti-thrombotic pathway in platelets. Agents derived from the inhibitory peptides described in this study may represent a new therapeutic strategy for anti-platelet or anti-integrin drug development