Solid state stacked trimers of 1,10-phenanthroline in a supramolecular tubular motif of C-methyl calix[4]resorcinarene

The self-assembly of bidentate ligand, 1,10-phenanthroline with C-methyl calix[4]resorcinarene (CMCR) in presence of coumarin results in a unique trimer stacking arrangement of phenanthroline molecules in a nanotubular motif generated by the supramolecular assembly of the host.

Copy of letter sent to Benjamin Pereira at Jamaica engaging him as teacher in K. K. S. I.

Digital image

Copy of letter of K. K. S. I. to London regarding selection of a hazan

Digital image

Draft of letter from Moses Seixas, Newport to K. K. S. I. regarding letter to President Washington

Digital image

Copy of letter from K. K. S. I. regarding sending money to Newport to help them build a synagogue

Digital image

Copy of letter from Portuguese congregation, London, to K. K. S. I. regarding re-burial of dead

Digital image

Copy of letter to Moses Franks regarding Hazan for K. K. S. I.

Digital image

Copy of letter and agreement with Mr. Solomons, shochet

Digital image

Draft of letter to Sir Moses Montefiore on the death of his wife

Digital image

Draft of letter by Jacques Judah Lyons to Sir Moses Montefiore, sending him payment for the Jews of Palestine, and acknowledgement

Digital image

Copy of letter from Jacques Judah Lyons to Sir Moses Montefiore enclosing bill of exchange for Palestinian Jews

Digital image

A cyclic peptide mimic of an RNA recognition motif of human La protein is a potent inhibitor of hepatitis C virus

Due to limited available therapeutic options, developing new lead compounds against hepatitis C virus is an urgent need. Human La protein stimulates hepatitis C virus translation through interaction with the hepatitis C viral RNA. A cyclic peptide mimicking the beta-turn of the human La protein that interacts with the viral RNA was synthesized. It inhibits hepatitis C viral RNA translation significantly better than the corresponding linear peptide at longer post-treatment times. The cyclic peptide also inhibited replication as measured by replicon RNA levels using real time RT-PCR. The cyclic peptide emerges as a promising lead compound against hepatitis C.

Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the alpha(1b)-adrenergic receptor: effects on receptor isomerization and activation.

We have suggested previously that both the negatively and positively charged residues of the highly conserved Glu/Asp-Arg-Tyr (E/DRY) motif play an important role in the activation process of the alpha(1b)-adreneric receptor (AR). In this study, R143 of the E/DRY sequence in the alpha(1b)-AR was mutated into several amino acids (Lys, His, Glu, Asp, Ala, Asn, and Ile). The charge-conserving mutation of R143 into lysine not only preserved the maximal agonist-induced response of the alpha(1b)-AR, but it also conferred high degree of constitutive activity to the receptor. Both basal and agonist-induced phosphorylation levels were significantly increased for the R143K mutant compared with those of the wild-type receptor. Other substitutions of R143 resulted in receptor mutants with either a small increase in constitutive activity (R143H and R143D), impairment (R143H, R143D), or complete loss of receptor-mediated response (R143E, R143A, R143N, R143I). The R413E mutant displayed a small, but significant increase in basal phosphorylation despite being severely impaired in receptor-mediated response. Interestingly, all the arginine mutants displayed increased affinity for agonist binding compared with the wild-type alpha(1b)-AR. A correlation was found between the extent of the affinity shift and the intrinsic activity of the agonists. The analysis of the receptor mutants using the allosteric ternary complex model in conjunction with the results of molecular dynamics simulations on the receptor models support the hypothesis that mutations of R143 can drive the isomerization of the alpha(1b)-AR into different states, highlighting the crucial role of this residue in the activation process of the receptor.

Club copy of letter of condolence to C. Morgan Arnold

A copy of a letter sent to a Mr. [C. Morgan] Arnold from the St. Catharines Garrison Club offering condolences on the death of his son, Major Henry M. Arnold, at the battle of Paardeberg, South Africa.