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106 items found (0 items not approved), displaying 1 to 10.[First/Prev] 1, 2, 3, 4, 5, 6, 7, 8 [Next/Last]

Instruments / Technical Area	Publication Details	Published	Actions
	A novel drug delivery approach for the formulation of lipophilic therapeutics of small molecule peptide-based and protein drugs Rohanah Hussain , Giuliano Siligardi 12th International Conference on Circular Dichroism	Aug 2009
	A novel cationic lipopeptide therapeutics with a broad range of antimicrobial activites Rohanah Hussain , Giuliano Siligardi 12th International Conference on Circular Dichroism	Aug 2009
	4-Fluoroproline derivative peptides: effect on PPII conformation and SH3 affinity Paolo Ruzza , Giuliano Siligardi , Arianna Donella-deana , Andrea Calderan , Rohanah Hussain , Chiara Rubini , Luca Cesaro , Alessio Osler , Andrea Guiotto , Lorenzo A. Pinna , Gianfranco Borin Journal Of Peptide Science 12 (7), 462-471 DOI: 10.1002/psc.750 PMID: 16506148 Show Abstract ▼ Abstract: Eukaryotic signal transduction involves the assembly of transient protein-protein complexes mediated by modular interaction domains. Specific Pro-rich sequences with the consensus core motif PxxP adopt the PPII helix conformation upon binding to SH3 domains. For short Pro-rich peptides, little or no ordered secondary structure is usually observed before binding interactions. The association of a Pro-rich peptide with the SH3 domain involves unfavorable binding entropy due to the loss of rotational freedom on forming the PPII helix. With the aim of stabilizing the PPII helix conformation in the Pro-rich HPKI decapeptide PPPLPPKPKF (P2), a series of P2 analogues was prepared, in which specific Pro positions were alternatively occupied by 4(S)- or 4(R)-4-fluoro-L-proline. The interactions of these peptides with the SH3 domain of the HPK1-binding partner HS1 were quantitatively analyzed by the NILIA-CD approach. A CD thermal analysis of the P2 analogues was performed to assess their propensity to adopt the PPII helix conformation. Contrary to our expectations, the K-d values of the analogues were lower than that of the parent peptide P2. These results clearly show that the induction of a stable PPII helix conformation in short Pro-rich peptides is not sufficient to increase their affinity toward the SH3 domain and that the effect of 4-fluoroproline strongly depends on the position of this residue in the sequence and the chirality of the substituent in the pyrrolidine ring. Copyright (c) 2006 European Peptide Society and John Wiley & Sons, Ltd.	Jul 2006
	Fat-free Albumin as a Novel Drug Delivery System Rohanah Hussain , Giuliano Siligardi International Journal Of Peptide Research And Therapeutics 12 (3), 311-315 DOI: 10.1007/s10989-006-9028-1 Show Abstract ▼ Abstract: The search for effective drug delivery systems is one of the major challenges in drug formulation especially for biopharmaceuticals Such as proteins, and peptide-based drugs and vaccines. A procedure has been developed whereby human serum albumin (HSA) call be Used as a delivery vehicle for these biomolecules using its role as main ratty acid carrier. Using essentially fatty acid free HSA (HSAff) it is possible to form stable complexes with lipidic chain compounds (lipo-compounds). Two lipo-compounds have been used to develop this system, a novel antimicrobial lipopeptide and gamma-amino-n-butyric acid, GABA. conjugated with an alkyl chain, lipo-GABA, in both cases C8 and C14 alkyl chain lengths were evaluated. The HAS-lipo compound complex had a mutual stabilizing effect on both the HSA and the lipo-compound. The protease enzyme study showed that the alkyl chains of these lipo-compounds bound to HSAff confer a similar if not greater biostability than caprylic acid shown by CD and importantly, the bound lipopeptide was stabilized by the HSA shown by mass spectrometry. Heat stability studies at 60 degrees C over 10 h also confirmed that the lipo-HSA complexes confer stability and provide a method of preparing sterile formulation for therapeutic use. No further increased in stability of the lipo-compounds when HSA containing fatty acid (HSAfa) Was used. With the antimicrobial lipopeptide, there was enhanced activity with HSAff formulation suggesting increased biostability and bioavailability of compounds. These finding allowed us to develop a simple and effective way of delivering lipo-compounds using fatty acid free HSA as the carrier.	Sep 2006
	Ligand interactions: Challenges ahead using SRCD Rohanah Hussain , Guiliano Siligardi 2nd International Workshop on Synchrotron Radiation Circular Dichroism Spectroscopy	Apr 2009
	Biomolecular Interactions of non immobilised systems by CD spectroscopy Rohanah Hussain , Giuliano Siligardi Chirality 2007	Jul 2007
	Design of B23 Circular Dichroism beamline at Diamond Light Source Rohanah Hussain , Giuliano Siligardi	Jul 2007
	Effect of 4-Fluoro-L-proline on the SH3 Binding Affinity Paolo Ruzza , Chiara Rubini , Andrea Calderan , Andrea Guiotto , Luca Cesaro , Anna M. Brunati , Arianna Donella-deana , Rohanah Hussain , Giuliano Siligardi Peptides For Youth: The Proceedings Of The 20th American Peptide Symposium 611, 499-500 DOI: 10.1007/978-0-387-73657-0_216 PMID: 19400283	Mar 2009
	Protein denaturation induced by vacuum UV radiation. Rohanah Hussain , Giuliano Siligardi International Conference on Materials for Advanced Technologies 2007	Jul 2007
	Identification and characterization of novel lipophilic antimicrobial peptides derived from naturally occurring proteins R. Hussain , C. L. Joannou , G. Siligardi International Journal Of Peptide Research And Therapeutics 12 (3), 269-273 6th Australian Peptide Conference DOI: 10.1007/s10989-006-9033-4 Show Abstract ▼ Abstract: Microbes are increasingly developing defensive mechanisms against known drugs via mutations. There are signs of emergence of superbugs immune to most known antibiotics available. The need for a new class of drugs to Counteract this problem is of paramount importance for continued general well being of mankind. A new class of drugs, antimicrobial peptides, has not been fully exploited primarily due to high cytotoxicity, poor lipophilicity preventing systemic distribution and stability. We have synthesised 9-amino acid residue cationic peptides RH01 and RH02 lipidated with myristoyl and octyl groups respectively. These peptides exhibited potent antimicrobial activity and low cytotoxicity. The lipopeptide RHO I has antimicrobial activity against a broad range of microorganisms including bacteria. yeast and filamentous fungi with greatest activity toward Gram-positive bacteria, including S. aureus MRSA stain, MIC's ranging between 2-8 mu M. The MIC for Gram-negative bacteria was higher ranging from between 30-250 mu M. RH01 also had antimicrobial activity towards fungi showing good activity against the pathogenic yeast Candida albicans but was less active towards the filamentous fungi Aspergillus niger. The antimicrobial activity of RH01 as a measure of Ki((50)) for E. coli and S. aureus was 35-60 mu M and 3-7 mu M, respectively. In-house data showed the compound is bactericidal even at higher bacteria concentration. The octylated lipopeptide RH02 has similar activities towards S. aureus (3.3 mu M) and E coli (53.3 mu M) as the myristolated RH01. There was no haemolytic activity of the lipopeptide RH01 towards human blood. Acute intravenous toxicity study in mice showed that both RH01 and RH02 induced no macroscopic abnormalities at their highest non-lethal dose of 75 mg/kg and 150 mg/kg bodyweight, respectively.	Sep 2006

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