The smooth muscle pharmacology of maximakinin, a receptor-selective, bradykinin-related nonadecapeptide from the venom of the Chinese toad, Bombina maxima.

Structural homologues of vertebrate regulatory peptides found in defensive skin secretions of anuran amphibians often display enhanced bioactivity and receptor binding when compared with endogenous mammalian peptide ligands. Maximakinin, a novel N-terminally extended bradykinin (DLPKINRKGPRPPGFSPFR) from the skin venom of a Chinese toad (Bombina maxima), displays such activity enhancement when compared with bradykinin but is additionally highly selective for mammalian arterial smooth muscle bradykinin receptors displaying a 50-fold increase in molar potency in this smooth muscle type. In contrast, a 100-fold decrease in molar potency was observed at bradykinin receptors in intestinal and uterine smooth muscle preparations. Maximakinin has thus evolved as a “smart” defensive weapon in the toad with receptor/tissue selective targeting. Natural selection of amphibian skin venom peptides for antipredator defence, through inter-species delivery by an exogenous secretory mode, produces subtle structural stabilisation modifications that can potentially provide new insights for the design of selectively targeted peptide therapeutics.

Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima

We have isolated a novel bradykinin B2-receptor antagonist peptide, kinestatin, from toad (Bombina maxima) defensive skin secretion. Mass spectroscopy established a molecular mass of 931.56 Da and a provisional structure: pGlu-Leu/Ile-Pro-Gly-Leu/Ile-Gly-Pro-Leu/Ile-Arg.amide. The unmodified sequence, -QIPGLGPLRG-, was located at the C-terminus of a 116-amino-acid residue open-reading frame following interrogation of a sequenced B. maxima skin cDNA library database. This confirmed the presence of appropriate primary structural attributes for the observed post-translational modifications present on the mature peptide and established residue 2 as Ile and residues 5/8 as Leu. Kinestatin represents a prototype novel peptide from amphibian skin.

Eighteen entries on Milton's Latin poetry

Entries on Elegia Prima, Elegia Quarta, Elegia Quinta, Elegia Sexta, Elegia Septima, In Quintum Novembris, Ad Salsillum, Mansus, Epitaphium Damonis, Apologus de Rustico & Hero, 5 entries on the Latin gunpowder epigrams, 3 entries on the Ad Leonoram epigrams.

Sporting with the Classics: The Latin Poetry of William Dillingham

Sporting with the Classics: The Latin Poetry of William Dillingham (2010) (back cover)

Dana Sutton, University of California:
‘The great merit of Estelle Haan's study is that she is willing to take Dillingham seriously as a poet. Her reproduction of his work, together with an English translation and very detailed studies of his individual poems have the combined effect of rescuing an interesting poet from near-total oblivion. This, in my opinion, is the finest thing a neo-Latin scholar can do, and Haan accomplishes her task with the same skill, sensitivity, and eloquence that have distinguished her studies of other neo-Latin poets of this period (Joseph Addison and Vincent Bourne). It is impossible not to react to this volume with extreme respect and appreciation’.

Gordon Campbell, University of Leicester:
‘Nothing substantial has ever been published on Dillingham, but with this volume we have a new corpus of poetry that intersects with the work of many other seventeenth-century neo-Latin and vernacular poets. Professor Haan’s scholarship is here (as always) placed at the service of the poet, and she leads the reader gently through the work of a new poet. Professor Haan is the most eminent and able neo-Latinist of her generation, and her scholarship never fails; sometimes it dazzles as in the chapters on the hangman's stone and on Renaissance topiary. Her research is always up-to-date, and her translations have a gracefulness that other laborers in the vineyard can only envy’.