Objectives/Background: Despite Cognitive Behavioral Therapy for Insomnia (CBT-I) being considered the first-line treatment for insomnia, it is not without its challenges. As such it is worthwhile to consider, and test, alternative or adjuvant management options. Methods/Participants: The aim of the present study was to examine whether Lucid Dreaming Training for insomnia (LDT-I) impacted on insomnia, depressive and anxious symptomology in an open label trial of 48 adults with Insomnia Disorder. Participants completed the Insomnia Severity Index, General Anxiety Disorder-7 and Patient Health Questionnaire at baseline then one month following LDT-I. Training consisted of four modules delivered over a period of two consecutive weeks. Results: The results suggest, albeit preliminarily, that LDT-I may have a place within the non-pharmacological management of insomnia, as there were significant reductions in insomnia severity (t(46) = 8.16,p <.001), anxious symptomology (t(46) = 4.75,p <.001) and depressive symptomology (t(46) = 5.87,p <.001). Further, the effect size in terms of pre-post reductions on ISI scores was large (d_z 1.17). Conclusions: Whilst the results are promising, further testing of LDT-I is needed to inform its place amongst the non-pharmacological treatments for insomnia.

27 May 2010·Journal of Medicinal ChemistryQ1 · MEDICINE

Leech-Derived Thrombin Inhibitors: From Structures to Mechanisms to Clinical Applications

Q1 · MEDICINE

Review

Author: Pereira, Pedro Jose Barbosa ; Fuentes-Prior, Pablo ; Macedo-Ribeiro, Sandra ; Corral-Rodriguez, Maria Angeles

A review.This paper discusses hirudin as a noncanonical inhibitor of thrombin, haemadin from the land-living leech Haemadipsa sylvestris and its targeting of thrombin exosite II, theromin and the factor Xa inhibitors antistasin and therostasin, leech-derived thrombin inhibitors as antithrombotic agents, and hirudin as a template for the design of novel antithrombotic agents.

01 Dec 2009·Journal of Biological ChemistryQ2 · BIOLOGY

Deciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase Inhibitor

Q2 · BIOLOGY

Article

Author: Joan L. Arolas ; David Pantoja-Uceda ; Jorge Santoro ; Francesc X. Aviles ; Christian P. Sommerhoff ; Salvador Ventura

Protein folding mechanisms have remained elusive mainly because of the transient nature of intermediates. Leech-derived tryptase inhibitor (LDTI) is a Kazal-type serine proteinase inhibitor that is emerging as an attractive model for folding studies. It comprises 46 amino acid residues with three disulfide bonds, with one located inside a small triple-stranded antiparallel beta-sheet and with two involved in a cystine-stabilized alpha-helix, a motif that is widely distributed in bioactive peptides. Here, we analyzed the oxidative folding and reductive unfolding of LDTI by chromatographic and disulfide analyses of acid-trapped intermediates. It folds and unfolds, respectively, via sequential oxidation and reduction of the cysteine residues that give rise to a few 1- and 2-disulfide intermediates. Species containing two native disulfide bonds predominate during LDTI folding (IIa and IIc) and unfolding (IIa and IIb). Stop/go folding experiments demonstrate that only intermediate IIa is productive and oxidizes directly into the native form. The NMR structures of acid-trapped and further isolated IIa, IIb, and IIc reveal global folds similar to that of the native protein, including a native-like canonical inhibitory loop. Enzyme kinetics shows that both IIa and IIc are inhibitory-active, which may substantially reduce proteolysis of LDTI during its folding process. The results reported show that the kinetics of the folding reaction is modulated by the specific structural properties of the intermediates and together provide insights into the interdependence of conformational folding and the assembly of native disulfides during oxidative folding.

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Indication	Highest Phase	Country/Location	Organization	Date
Cicatrix	Discovery	DE	tiakis BIOTECH AG	-
Inflammation	Discovery	DE	tiakis BIOTECH AG	-

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