Boston University

Periodontix, Inc.

Other

Frank G Oppenheim

Tao Xu

F Donald Roberts

Peter Spacciapoli

Phillip M Friden

Eva J Helmerhorst

There are gluten-degrading enzymes found inspecies bacteria that are capable of breaking peptide bonds in -XPQ-, -QQP-, -PPF-, -LYP- and/or -PFP-containing peptides. These enzymes are acidic enzymes; they retain protease activity at acidic pH, eg., at 3.0, and have isoelectric points in a pH range of 2.0-7.0. Embodiments herein provide isolated enzyme compositions and probiotic compositions comprising at least one acidic gluten-degrading enzyme or aspecies bacteria. Also provided herein are methods of treatment of celiac disease or a related disorder, treatment of gluten-containing foodstuff, degrading and/or detoxifying gluten comprising the acidic gluten-degrading enzyme and/or compositions.

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The invention relates to glutamine endopeptidase enzymes fromspp. bacteria that are naturally associated with the oral cavity, formulations comprising the glutamine endopeptidase enzymes and the use thereof for the treatment, prevention of allergic reaction and diagnosis of gluten allergy related diseases such as Celiac Sprue, gluten allergy and/or dermatitis herpetiformis.

Substantially pure peptides containing between 13 and 20 amino acids, inclusive, having the amino acid sequence: R1-R2-R3-R4-R5-R6-R7-R8-R9-R10-R11-R12-R13-R14-R15-R16-R17-R18-R19-R20-R21-R22-R23, where R1 is Asp or is absent; R2 is Ser or is absent; R3 is His or is absent; R4 is Ala; R5 is Lys, Gln, Arg, or another basic amino acid; R6 is Arg, Gln, Lys, or another basic amino acid; R7 is His, Phe, Tyr, Leu, or another hydrophobic amino acid; R8 is His, Phe, Tyr, Leu, or another hydrophobic amino acid; R9 is Gly, Lys, Arg, or another basic amino acid; R10 is Tyr; R11 is Lys, His, Phe, or another hydrophobic amino acid; R12 is Arg, Gln, Lys, or another basic amino acid; R13 is Lys, Gln, Arg, another basic amino acid, or is absent; R14 is Phe or is absent; R15 is His, Phe, Tyr, Leu, another hydrophobic amino acid, or is absent; R16 is Glu or is absent; R17 is Lys or is absent; R18 is His or is absent; R19 is His or is absent; R20 is Ser or is absent; R21 is His or is absent; R22 is Arg or is absent; and R23 is Gly or is absent; and where Gln cannot simultaneously occupy positions R5, R6, R12, and R13 of the amino acid sequence, as well as pharmaceutical compositions containing these peptides and methods for treating fuingal and bacterial infections using these peptides, are disclosed.

Antifungal and antibacterial peptides

Anti-fungal and anti-bacterial histatin-based peptides

Anti-fungal D-amino acid histatin-based peptides

Peptides representing defined portions of the amino acid sequences of naturally occurring human and macaque histatins, modified peptides, expression vectors encoding these peptides, and compositions and methods for treatment of fungal infection are described. Some of the histatin-based peptides exhibit superior anti-fungal activity to native, intact histatins. Isolated, naturally occurring macaque histatins and peptide analogs are also described.

Methods of treating fungal infections using histatin-based peptides

D-amino acid histatins and histatin-based peptides histatins and methods for treatment of fungal or bacterial infection are described. These D-amino acid histatins and histatin-based peptides are longer-acting anti-fungal or anti-bacterial agents than their L-enantiomeric analogues.

D-amino acid histatin-based peptides as anti-fungal and anti-bacterial

Histatin-based peptides representing defined portions of the amino acid sequences of naturally occurring human histatins and methods for treatment of fungal or bacterial infection are described. These histatin-based peptides represent the active anti-fungal and anti-bacterial region of naturally occurring human histatins.

Growing community of inventors

Chestnut Hill, MA, United States of America

Frank G Oppenheim