Calamities causing loss of museum collections: a historical and global perspective on museum disasters.

With alarming frequency, significant collections in natural history museums have been destroyed or damaged through insurrections, cyclones, wars, fires, floods, or earthquakes particularly in the nineteenth century but continuing into the twentieth century with World War II bombings, fires, and earthquakes being the primary causes of loss in fifty-seven institutions across thirty countries. We review the loss or damage of museum collections globally, and their varied causes. We emphasize the benefits of dispersal of a sample of paratypes across institutions as an essential feature of taxonomic practice.

Inhibition of HIV infection by caerin 1 antimicrobial peptides.

The major mode of transmission of the human immunodeficiency virus (HIV) is by sexual intercourse. In the effort to halt the spread of HIV, one measure that holds great promise is the development of effective microbicides that can prevent transmission. Previously we showed that several amphibian antimicrobial peptides (AMPs) completely inhibit HIV infection of T cells while maintaining good viability of the T cell targets.

The adhesive skin exudate of Notaden bennetti frogs (Anura: Limnodynastidae) has similarities to the prey capture glue of Euperipatoides sp. velvet worms (Onychophora: Peripatopsidae).

The dorsal adhesive secretion of the frog Notaden bennetti and the prey-capture "slime" ejected by Euperipatoides sp. velvet worms look and handle similarly. Both consist largely of protein (55-60% of dry weight), which provides the structural scaffold.

Host-defense peptides of Australian anurans. Part 2. Structure, activity, mechanism of action, and evolutionary significance.

A previous review summarized research prior to 2004 carried out on the bioactive host-defense peptides contained in the skin secretions of Australian anurans (frogs and toads). This review covers the extension of that research from 2004 to 2012, and includes membrane-active peptides (including antibacterial, anticancer, antifungal and antiviral peptides) together with the mechanisms by which these peptides interact with model membranes, peptides that may be classified as "neuropeptides" (including smooth muscle active peptides, opioids and immunomodulators) and peptides which inhibit the formation of nitric oxide from neuronal nitric oxide synthase. The review discusses the outcome of cDNA sequencing of signal-spacer-active peptides from an evolutionary viewpoint, and also lists those peptides for which activities have not been found to this time.

An unusual kynurenine-containing opioid tetrapeptide from the skin gland secretion of the Australian red tree frog Litoria rubella. Sequence determination by electrospray mass spectrometry.

The Kyn-containing peptide FP-Kyn-L(NH(2)) is an unusual minor component of the skin peptide profile of the Australian red tree frog Litoria rubella collected from an area within a 20 kilometre radius of Alice Springs in central Australia. The structure was determined by electrospray mass spectrometry and synthesis. The major component of the skin secretion is the analogous tryptophyllin peptide FPWL(NH(2)).

Skin peptide and cDNA profiling of Australian anurans: genus and species identification and evolutionary trends.

Host defense peptides of 35 species of Australian frogs from the hylids Cyclorana and Litoria, and the myobatrachids Crinia, Limnodynastes and Uperoleia have been identified. The biological activities of the majority of these peptides have been determined and include hormones, neuropeptides, opioids, immunomodulators, membrane active peptides [including antimicrobial, anticancer, antiviral (enveloped viruses like HIV and Herpes) and antifungal peptides], neuronal nitric oxide synthase inhibitors, pheromones and individual peptides with other specific activities. The host defense peptide skin profile can be diagnostic at both the species and higher taxonomic levels; for example, species of Crinia, Litoria and Uperoleia each produce quite different types of peptides.

The host-defence skin peptide profiles of Peron's Tree Frog Litoria peronii in winter and summer. Sequence determination by electrospray mass spectrometry and activities of the peptides.

Positive and negative ion electrospray mass spectrometry together with Edman sequencing (when appropriate) has been used to sequence the host-defence peptides secreted from skin glands of the tree frog Litoria peronii. The peptide profiles are different in winter and summer. In winter, the frog produces small amounts of the known caerin 1.

Biocompatibility and modification of the protein-based adhesive secreted by the Australian frog Notaden bennetti.

When provoked, Notaden bennetti frogs secrete a proteinaceous exudate, which rapidly forms a tacky and elastic glue. This material has potential in biomedical applications. Cultured cells attached and proliferated well on glue-coated tissue culture polystyrene, but migrated somewhat slower than on uncoated surfaces.

Skin peptides from anurans of the Litoria rubella Group: sequence determination using electrospray mass spectrometry. Opioid activity of two major peptides.

Many species of frogs of the genus Litoria secrete bioactive peptides from their skin glands. These peptides are normally host-defence compounds and may have one, or more of the following activities; smooth muscle contraction, analgesic, antimicrobial, antiviral, lymphocyte proliferator (immunomodulator) and neuronal nitric oxide synthase (nNOS) inactivation. Two frog species of the Litoria rubella Group that have been studied before, namely, Litoria electrica and Litoria rubella, are different from other species of the genus Litoria in that they produce small peptides that show neither membrane, lymphocyte nor nNOS activity.

Frog glue enhances rotator cuff repair in a laboratory cadaveric model.

Summary: Rotator cuff tendons are typically reattached to the proximal humerus using transosseous sutures or suture anchors. Their primary mode of failure is at the tendon-bone interface. We investigated the addition of a novel adhesive secreted from a species of Australian frog (Notaden bennetti) to different methods of rotator cuff repair.

The fallaxidin peptides from the skin secretion of the Eastern Dwarf Tree Frog Litoria fallax. Sequence determination by positive and negative ion electrospray mass spectrometry: antimicrobial activity and cDNA cloning of the fallaxidins.

The glandular skin secretion of the Eastern Dwarf Tree Frog Litoria fallax contains nine peptides named fallaxidins. The sequences of these peptides were elucidated using a combination of positive and negative electrospray mass spectrometry together with Edman sequencing. Among these peptides are: (i) fallaxidins 1.

Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: structure, activity and evolutionary trends.

The skin secretions of Crinia signifera, C. riparia and C. deserticola contain bioactive disulfide-containing peptides.

Host-defence peptide profiles of the skin secretions of interspecific hybrid tree frogs and their parents, female Litoria splendida and male Litoria caerulea.

Five healthy adult female first-generation hybrid tree frogs were produced by interspecific breeding of closely related tree frogs Litoria splendida and L. caerulea in a cage containing large numbers of males and females of both species. Phylogenetic analysis of mitochondrial DNA sequences established the female parent to be L.

New caerin antibiotic peptides from the skin secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification using positive and negative ion electrospray mass spectrometry.

The skin secretion of the Dainty Green Tree Frog Litoria gracilenta contains 16 peptides, which protect the animal from predators, both large and small. A combination of negative and positive ion electrospray mass spectrometry together with Lys-C enzymic digest and Edman sequencing identifies three new wide-spectrum caerin 1 antibiotics, namely Caerin 1.17 [GLFSVLGSVAKHLLPHVAPIIAEKL-NH2], Caerin 1.

Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry.

A combination of positive and negative ion electrospray mass spectrometry (ES-MS) together with automated Edman sequencing has been used to determine the amino acid sequences of the host-defence peptides from the skin glands of the froglet Crinia riparia. The peptides are called riparins. Of the eight peptides isolated, five are neuropeptides containing intramolecular disulfide linkages; e.

Population trends associated with skin peptide defenses against chytridiomycosis in Australian frogs.

Many species of amphibians in the wet tropics of Australia have experienced population declines linked with the emergence of a skin-invasive chytrid fungus, Batrachochytrium dendrobatidis. An innate defense, antimicrobial peptides produced by granular glands in the skin, may protect some species from disease. Here we present evidence that supports this hypothesis.

Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells.

Topical antimicrobicides hold great promise in reducing human immunodeficiency virus (HIV) transmission. Amphibian skin provides a rich source of broad-spectrum antimicrobial peptides including some that have antiviral activity. We tested 14 peptides derived from diverse amphibian species for the capacity to inhibit HIV infection.

The rothein peptides from the skin secretion of Roth's tree frog Litoria rothii. Sequence determination using positive and negative ion electrospray mass spectrometry.

The secretion from the dorsal glands of the frog Litoria rothii contains a series of new peptides including rothein 1 (SVSNIPESIGF-OH, a neuropeptide which contracts smooth muscle), a number of inactive rothein 2 and 3 peptides (e.g. rothein 2.

Host-defence skin peptides of the Australian Common Froglet Crinia signifera: sequence determination using positive and negative ion electrospray mass spectra.

The amino acid sequences of seven signiferin peptides are provided by consideration of tandem mass spectrometric (MS/MS) data for the respective MH+ and [M--H]- precursor ions. These methods do not differentiate between isomeric residues Leu and Ile; these were identified using the Edman degradation technique. The sequence of signiferin 1, a new smooth muscle contracting neuropeptide (RLCIPYIIPC-OH) containing a disulfide bridge, is best determined using the collision-induced dissociation (CID) spectrum of the [M--H]- anion.

Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.

Host-defence peptides secreted from the skin glands of Australian frogs and toads, are, with a few notable exceptions, different from those produced by anurans elsewhere. This review summarizes the current knowledge of the following classes of peptide isolated and characterized from Australian anurans: neuropeptides (including smooth muscle active peptides, and peptides that inhibit the production of nitric oxide from neuronal nitric oxide synthase), antimicrobial and anticancer active peptides, antifungal peptides and antimalarial peptides. Other topics covered include sex pheromones of anurans, and the application of peptide profiling to (i).

Chemical and olfactory characterization of odorous compounds and their precursors in the parotoid gland secretion of the green tree frog, Litoria caerulea.

When stressed or challenged by a predator, the Australian green tree frog, Litoria caerulea, emits a characteristic nutty odor from its parotoid glands. This study identifies the source of the odor as the cyclic amide 2-pyrrolidone (2-PyrO). In addition, we demonstrate the presence of 2-PyrO's straight chain form, gamma-aminobutyric acid or GABA, in the frog's glandular secretion and propose an odorant-precursor relationship.

nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified citropin 1.1.

A large number of bioactive peptides have been isolated from amphibian skin secretions. These peptides have a variety of actions including antibiotic and anticancer activities and the inhibition of neuronal nitric oxide synthase. We have investigated the structure-activity relationship of citropin 1.

Negative ion electrospray mass spectra of caerulein peptides: an aid to structural determination.

MS/MS data derived from the [M-H](-) ions of desulfated caerulein peptides provide (i) sequencing information from a combination of alpha, beta and gamma backbone cleavages, and (ii) identification of specific amino acid side chains by side-chain cleavages [e.g. Ser (-CH(2)O), Thr (-CH(3)CHO) and Asp (-H(2)O)] (fragmentations having no counterparts in positive ion spectra).