Dr Laila Huq
Dr. Laila Huq
BSc Hons Coordinator
Education Program Leader Oral Health CRC
Bio21 30 Flemington Rd
The University of Melbourne
Victoria 3010 Australia
Telephone: +61 3 8344 2574
QUALIFICATIONS AND POSITIONS
- 1979-1982 B.Sc., University of Auckland.
- 1982-1984 M.Sc., Hons. 1st class, University of Auckland.
- 1984-1988 Ph.D., University of New South Wales.
- B.Sc. Honours Coordinator.
- Education Program Leader Oral Health CRC.
CURRENT RESEARCH INTERESTS
(Projects that are available for BSc Honours, MSC, and PhD students are indicated by an asterisk*)
- Nanotechnology: Structure-Function Studies of Casein Phosphopeptides.*
- Structure-function studies and biomimetics of phosphorylated peptides and proteins.*
- Structure-function studies of salivary proteins.*
- Salivary Informatics.*
- Identification of bioactive peptides from milk.*
- Evolutionary Bioinformatics of Cysteine Protease and Protease Inhibitors.
PhD projects available at Melbourne Dental School
Natural inhibitors of bacterial pathogen proteases
This is an opportunity for highly motivated and enthusiastic students to undertake a multidisciplinary research project that has commerciallization potential.
Contact Dr Laila Huq email: firstname.lastname@example.org
Australians and NZ citizens
- There are no tuition fees.
- You will be assessed on your academic abilities to undertake a research project.
- If you have an Australian Postgraduate Scholarship or equivalent, you may also apply for an Oral Health CRC top-up scholarship.
- There are no tuition fees, if you have a guaranteed scholarship from your country that covers your living expenses.
- You may eligible for a highly competitive Melbourne International Research scholarship
- If you do not hold a scholarship you will need to pay tuition fees of approx $32,000 every year
- To see Dr Huq's publications please visit her Find an Expert page
- Mineralized Tissue, International Association for Dental Research.
- Australasian Proteomics Society
- Undergraduate: Biomineralisation of Dentine and Enamel, Salivary Proteins
- Postgraduate Common Core: Bioinformatics and Cheminformatic
My research interests encompass the structure-function studies of proteins and peptides with diagnostic or therapeutic potential . Early graduate and post-graduate research include the structure [2-4], immunochemistry , paleobiochemistry , and clinical studies   of a small post-translationally modified protein osteocalcin used as a diagnostic in bone disorders.
Post-doctoral investigations involve Resonance Raman Spectroscopy  and electrochemical techniques  successfully applied to selected metalloproteins, and molecular modelling of post-translationally modified protein derived from a pathogen . My interest in the structure-function relationships of proteins continues today with an emphasis on characterising proteins, peptides, and biomimetic peptides for therapeutic development for oral health. The research includes the purification , characterisation [13, 14] and structural studies  of a highly post-translationally modified protein phosphophoryn and the synthesis  and structural studies of a phosphophoryn derived biomimetic peptide  with potential in dentine repair.
The multi-disciplinary research describing the purification, characterisation [19, 20], structural studies [21-24], and molecular modelling [25-27] of casein phosphopeptides (CPP) has demonstrated that the non-toxic and biocompatible CPP self-assemble and encapsulate the calcium and phosphate mineral in the form of amorphous calcium phosphate (ACP) thus forming CPP-ACP nanocomplexes. The biomedical application is the demonstrated repair of tooth surfaces at early stages of tooth decay. This research has contributed to the scientific evidence for the currently commerciallized CPP-ACP ingredient found in sugar-free gum (Trident XtraCare with Recaldent), professional tooth crème (GC's Tooth Mousse, MI Paste, and MI Paste Plus), and dairy milk (Meiji Milk de Recaldent). (http://en.wikipedia.org/wiki/Recaldent). The long-term goal is to improve the design and efficacy of non-toxic self-assembling, biocompatible, delivery vehicles for mineral ions with current applications in the biomedical, health and pharmaceutical industry.
My research interests also include the diagnostic and therapeutic potential of saliva. This is highlighted by the research describing the diagnostic potential of salivary pH for clinical applications [31, 32], evolution of salivary proteins , the salivary peptidome , and the recent emergence of saliva-derived peptide therapeutics.
Our tradition of sourcing bioactive peptides from natural products led to the screening of casein peptides for inhibitory activity against the virulent outer membrane protease gingipains of the oral pathogen P. gingivalis. These studies enabled the discovery of inhibitory peptides derived from milk caseins [[34, 35] & patent PCT/AU/2010/000760].
I am also interested in the evolutionary relationships and different inhibitory mechanisms of known cysteine protease inhibitors and its relationship to modern chemotherapeutic design for the treatment of infectious diseases . My interest in molecular evolution of proteins and the effect on structure-function relationships continues with the current investigation of the use of the propeptide as an effective inhibitor of the oral pathogen P. gingivalis gingipains [provisional patent 2010/902955].
1. Teh LC, et al. (1987). J Biol Chem 262:6472-6477.
2. Huq NL, et al. (1984). Biochem Int 8:521-527.
3. Mende LM, et al. (1984). Int J Pept Prot Res 24:297-302.
4. Huq NL, et al. (1987). Biochem Int 15:271-277.
5. Huq NL, et al. (1985). Biochem Biophys Res Commun 129:714-720.
6. Huq NL, et al. (1990). Biochem Int 21:491-496.
7. Reid IR, et al. (1986). J Clin Endocrinol Metab 62:379-383.
8. Pocock NA, et al. (1987). Ann Intern Med 107:319-323.
9. Han J, et al. (1991). Biochemistry-US 30:10904-10913.
10. Buchi FN, et al. (1992). Inorg Chem 31:5007-5014.
11. Dashper SG, et al. (1994). Biochem Biophys Res Commun 199:1297-1304.
12. Huq NL, et al. (2000). J Dent Res 79:1914-1919.
13. Huq NL, et al. (2005). Arch Oral Biol 50:807-819.
14. Huq NL, et al. (2005). Arch Oral Biol 50:599-609.
15. Cross KJ, et al. (2005). J Pept Res 66:59-67.
16. O'Brien-Simpson NM, et al. (2007). Int J Pept Res Ther 13:469-478.
17. Cross KJ, et al. (2007). Int J Pept Res Ther 13:479-495.
18. Huq NL, et al. (1995). Biochim Biophys Acta 1247:201-208.
19. Perich JW, et al. (1999). J Pept Sci 5:221-233.
20. Reynolds EC, et al. (1999). J Clin Dent 10:86-88.
21. Cross KJ, et al. (2001). Biochem J 356:277-286.
22. Huq NL, et al. (2003). J Pept Sci 9:386-392.
23. Cross KJ, et al. (2004). Biomaterials 25:5061-5069.
24. Cross KJ, et al. (2005). J Biol Chem 280:15362-15369.
25. Cross KJ, et al. (1997). J Dent Res 76:1661-1661.
26. Huq NL, et al. (2000). J Mol Model 6:35-47.
27. Huq NL, et al. (2004). J Dairy Res 71:28-32.
28. Cross KJ, et al. (2006) Anticariogenic Peptides. In: Mine Y, Shahidi F, eds. Nutraceutical Proteins and Peptides in Health and Disease. Vol. 4. Boca Raton: Taylor and Francis,335-352.
29. Cochrane NJ, et al. (2010). J Dent Res 89:1187-1197.
30. Cross KJ, et al. (2007). CurrPharm Des 13:793-800.
31. Kitasako Y, et al. (2008). Aust Dent J 53:140-144.
32. Kitasako Y, et al. (2009). Oral Surg, Oral Med, Oral Path, Oral Rad, and Endo 108:551-556.
33. Huq NL, et al. (2007). Int J Pept Res Ther 13:547-564.
34. Toh EC, et al. (2011). Antimicrob Agents Chemother
35. Toh ECY, et al. (2012). Inter Dairy J
36. Toh EC, et al. (2010). Curr Protein Pept Sci 11:725-743.