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Article: Design and modification of frog skin peptide brevinin-1GHa with enhanced antimicrobial activity on Gram-positive bacterial strains

Kara, Şeyda / Kürekci, Cemil / Akcan, Muharrem

Amino acids. 2022 Sept., v. 54, no. 9

2022

Abstract: Naturally occurring frog skin peptides are one of largest sources of antimicrobial peptides that have many advantages including high potency, broad spectrum of targets and low susceptibility to multiple drug-resistance bacteria. However, they also have ... ...

Abstract	Naturally occurring frog skin peptides are one of largest sources of antimicrobial peptides that have many advantages including high potency, broad spectrum of targets and low susceptibility to multiple drug-resistance bacteria. However, they also have disadvantages such as hemolytic activity, low stability and high production costs. For these reasons, various strategies have been applied to overcome these drawbacks restricting their use in clinical trials. Previously reported brevinin-1GHa (BR-1GHa) is a 24 amino acid long antimicrobial peptide isolated from Hylarana guentheri with hemolytic activity. To enhance the antimicrobial activity of this peptide and to reduce its hemolytic activity, we designed five new temporin like analogues and examined their bioactivities. Temporins are another class of frog skin peptides without hemolytic activity and shorter than brevinins. When the antimicrobial activities of new analogues were examined against a panel of microorganisms, BR-1GHa-3, in which two alanine residues in the truncated version of BR-1GHa were replaced with leucine, exhibited significantly improved antimicrobial activity against Gram-positive bacterial strains (e.g., S. aureus ATCC 29213 and E. casseliflavus ATCC 700327) with lower hemolytic activity compared to the BR-1GHa peptide. Furthermore, BR-1GHa-4 analogue, in which Gly3 was replaced with Pro, did not show any hemolytic activity except for highest (128 µM) concentration tested and have a strong antimicrobial effect on Gram-positive bacteria (e.g., E. faecalis ATCC 51299 and B. cereus ATCC 13061).
Keywords	Bacillus cereus ; Gram-positive bacteria ; alanine ; antimicrobial peptides ; antimicrobial properties ; frogs ; hemolysis ; leucine
Language	English
Dates of publication	2022-09
Size	p. 1327-1336.
Publishing place	Springer Vienna
Document type	Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-022-03189-7
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Article ; Online: Design and modification of frog skin peptide brevinin-1GHa with enhanced antimicrobial activity on Gram-positive bacterial strains.

Kara, Şeyda / Kürekci, Cemil / Akcan, Muharrem

Amino acids

2022 Volume 54, Issue 9, Page(s) 1327–1336

Abstract	Naturally occurring frog skin peptides are one of largest sources of antimicrobial peptides that have many advantages including high potency, broad spectrum of targets and low susceptibility to multiple drug-resistance bacteria. However, they also have disadvantages such as hemolytic activity, low stability and high production costs. For these reasons, various strategies have been applied to overcome these drawbacks restricting their use in clinical trials. Previously reported brevinin-1GHa (BR-1GHa) is a 24 amino acid long antimicrobial peptide isolated from Hylarana guentheri with hemolytic activity. To enhance the antimicrobial activity of this peptide and to reduce its hemolytic activity, we designed five new temporin like analogues and examined their bioactivities. Temporins are another class of frog skin peptides without hemolytic activity and shorter than brevinins. When the antimicrobial activities of new analogues were examined against a panel of microorganisms, BR-1GHa-3, in which two alanine residues in the truncated version of BR-1GHa were replaced with leucine, exhibited significantly improved antimicrobial activity against Gram-positive bacterial strains (e.g., S. aureus ATCC 29213 and E. casseliflavus ATCC 700327) with lower hemolytic activity compared to the BR-1GHa peptide. Furthermore, BR-1GHa-4 analogue, in which Gly3 was replaced with Pro, did not show any hemolytic activity except for highest (128 µM) concentration tested and have a strong antimicrobial effect on Gram-positive bacteria (e.g., E. faecalis ATCC 51299 and B. cereus ATCC 13061).
MeSH term(s)	Amino Acid Sequence ; Amphibian Proteins/chemistry ; Animals ; Anti-Bacterial Agents/pharmacology ; Anti-Infective Agents/chemistry ; Gram-Positive Bacteria ; Hemolysis ; Microbial Sensitivity Tests ; Ranidae ; Skin/metabolism ; Staphylococcus aureus
Chemical Substances	Amphibian Proteins ; Anti-Bacterial Agents ; Anti-Infective Agents
Language	English
Publishing date	2022-07-19
Publishing country	Austria
Document type	Journal Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-022-03189-7
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Article: Cyclotide-rich fractions containing nanofibers by electrospinning: preparation, characterization and examination of antimicrobial activity.

Baş, Elif Büşra / Kürekci, Cemil / Kalfa, Orhan Murat / Akcan, Muharrem

Turkish journal of chemistry

2022 Volume 46, Issue 5, Page(s) 1651–1660

Abstract: In this study, antimicrobial nanofibers were produced with the mixtures of polyvinyl alcohol (PVA) and cyclotide-rich fractions by electrospinning method. After extraction, the first separation was carried out with C18 flash chromatography and then ... ...

Abstract	In this study, antimicrobial nanofibers were produced with the mixtures of polyvinyl alcohol (PVA) and cyclotide-rich fractions by electrospinning method. After extraction, the first separation was carried out with C18 flash chromatography and then fractioned into five separate parts by reversed-phase high-pressure liquid chromatography (RP-HPLC). The molecular weights of cyclotides in each fraction were determined by quadrupole time-of-flight liquid chromatography-mass spectrometry (Q-TOF LC-MS). Cyclotide-rich fractions were mixed with 10% of PVA solution and nanofibers were produced from this biocomposite mixture by electrospinning method. The nanofibers were characterized by field emission scanning electron microscopy (FE-SEM), and it was observed that 100% peptide-containing nanofibers (cyclotide-rich fraction/10% PVA, w/v) had more regular fiber textures. The presence of the peptides in the nanofiber was also confirmed by analytical RP-HPLC, as the peptides in both peptide fractions and nanofiber solutions have the same retention times. The nanofibers produced with the fourth cyclotide-rich fraction showed activity against gram-positive bacteria (
Language	English
Publishing date	2022-07-19
Publishing country	Turkey
Document type	Journal Article
ZDB-ID	2046471-X
ISSN	1303-6130 ; 1300-0527
ISSN (online)	1303-6130
ISSN	1300-0527
DOI	10.55730/1300-0527.3468
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Article ; Online: Synthesis of cyclic disulfide-rich peptides.

Akcan, Muharrem / Craik, David J

Methods in molecular biology (Clifton, N.J.)

2013 Volume 1047, Page(s) 89–101

Abstract: In this chapter we describe two SPPS approaches for producing cyclic disulfide-rich peptides in our laboratory, including cyclotides from plants, cyclic conotoxins from cone snail venoms, chlorotoxin from scorpion venom, and the sunflower trypsin ... ...

Abstract	In this chapter we describe two SPPS approaches for producing cyclic disulfide-rich peptides in our laboratory, including cyclotides from plants, cyclic conotoxins from cone snail venoms, chlorotoxin from scorpion venom, and the sunflower trypsin inhibitor peptide, SFTI-1.
MeSH term(s)	Amino Acids/chemistry ; Disulfides/chemistry ; Fluorenes/chemistry ; Formic Acid Esters/chemistry ; Peptides, Cyclic/chemical synthesis ; Peptides, Cyclic/chemistry ; Solid-Phase Synthesis Techniques/methods
Chemical Substances	Amino Acids ; Disulfides ; Fluorenes ; Formic Acid Esters ; Peptides, Cyclic ; t-butyloxycarbonyl group
Language	English
Publishing date	2013
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-62703-544-6_6
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Article ; Online: The three-dimensional solution structure of mini-M conotoxin BtIIIA reveals a disconnection between disulfide connectivity and peptide fold.

Akcan, Muharrem / Cao, Ying / Chongxu, Fan / Craik, David J

Bioorganic & medicinal chemistry

2013 Volume 21, Issue 12, Page(s) 3590–3596

Abstract: Conotoxins are bioactive peptides from the venoms of marine snails and have been divided into several superfamilies based on homologies in their precursor sequences. The M-superfamily conotoxins can be further divided into five branches based on the ... ...

Abstract	Conotoxins are bioactive peptides from the venoms of marine snails and have been divided into several superfamilies based on homologies in their precursor sequences. The M-superfamily conotoxins can be further divided into five branches based on the number of residues in the third loop of the peptide sequence. Recently two M-1 branch conotoxins (tx3a and mr3e) with a C1-C5, C2-C4, C3-C6 disulfide connectivity and one M-2 branch conotoxin (mr3a) with a C1-C6, C2-C4, C3-C5 disulfide connectivity were described. Here we report the disulfide connectivity, chemical synthesis and the three-dimensional NMR structure of the novel 14-residue conotoxin BtIIIA, extracted from the venom of Conus betulinus. It has the same disulfide connectivity as mr3a, which puts it in the M-2 branch conotoxins but has a distinctly different structure from other M-2 branch conotoxins. 105 NOE distance restraints and seven dihedral angle restraints were used for the structure calculations. The three-dimensional structure was determined with CYANA based on torsion angle dynamics and refinement in a water solvent box was carried out with CNS. Fifty structures were calculated and the 20 lowest energy structures superimposed with a RMSD of 0.49±0.16 Å. Even though it has the M-2 branch disulfide connectivity, BtIIIA was found to have a 'flying bird' backbone motif depiction that is found in the M-1 branch conotoxin mr3e. This study shows that conotoxins with the same cysteine framework can have different disulfide connectivities and different peptide folds.
MeSH term(s)	Conotoxins/chemical synthesis ; Conotoxins/chemistry ; Disulfides/chemistry ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Protein Folding ; Solutions
Chemical Substances	Conotoxins ; Disulfides ; Solutions
Language	English
Publishing date	2013-06-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2013.02.012
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Article: The three-dimensional solution structure of mini-M conotoxin BtIIIA reveals a disconnection between disulfide connectivity and peptide fold

Akcan, Muharrem / Cao, Ying / Chongxu, Fan / Craik, David J

Bioorganic & medicinal chemistry. 2013 June 15, v. 21, no. 12

2013

Abstract	Conotoxins are bioactive peptides from the venoms of marine snails and have been divided into several superfamilies based on homologies in their precursor sequences. The M-superfamily conotoxins can be further divided into five branches based on the number of residues in the third loop of the peptide sequence. Recently two M-1 branch conotoxins (tx3a and mr3e) with a C1–C5, C2–C4, C3–C6 disulfide connectivity and one M-2 branch conotoxin (mr3a) with a C1–C6, C2–C4, C3–C5 disulfide connectivity were described. Here we report the disulfide connectivity, chemical synthesis and the three-dimensional NMR structure of the novel 14-residue conotoxin BtIIIA, extracted from the venom of Conus betulinus. It has the same disulfide connectivity as mr3a, which puts it in the M-2 branch conotoxins but has a distinctly different structure from other M-2 branch conotoxins. 105 NOE distance restraints and seven dihedral angle restraints were used for the structure calculations. The three-dimensional structure was determined with CYANA based on torsion angle dynamics and refinement in a water solvent box was carried out with CNS. Fifty structures were calculated and the 20 lowest energy structures superimposed with a RMSD of 0.49±0.16Å. Even though it has the M-2 branch disulfide connectivity, BtIIIA was found to have a ‘flying bird’ backbone motif depiction that is found in the M-1 branch conotoxin mr3e. This study shows that conotoxins with the same cysteine framework can have different disulfide connectivities and different peptide folds.
Keywords	bioactive properties ; cysteine ; energy ; nuclear magnetic resonance spectroscopy ; peptides ; snails ; solvents ; synthesis ; venoms
Language	English
Dates of publication	2013-0615
Size	p. 3590-3596.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2013.02.012
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Article: Cyclization of conotoxins to improve their biopharmaceutical properties

Clark, Richard J / Akcan, Muharrem / Kaas, Quentin / Daly, Norelle L / Craik, David J

Toxicon. 2012 Mar. 15, v. 59, no. 4

2012

Abstract: Conotoxins are disulfide-rich peptides from the venoms of marine cone snails that are used in prey capture. Due to their exquisite potency and selectivity for different ion channels, receptors and transporters they have attracted much interest as leads ... ...

Abstract	Conotoxins are disulfide-rich peptides from the venoms of marine cone snails that are used in prey capture. Due to their exquisite potency and selectivity for different ion channels, receptors and transporters they have attracted much interest as leads in drug design. This article gives a brief background on conotoxins, describes their structures and highlights methods for synthetic cyclization to improve their biopharmaceutical properties. The proximity of the N and C termini of many conotoxins makes them particularly suitable for cyclization with linkers of on average five to seven amino acids. By linking the ends of conotoxins it is possible to significantly decrease their susceptibility to proteolysis without loss of their intrinsic biological activity. Here, the principles of conotoxin cyclization are illustrated with applications to the α- and χ- conotoxin classes, which have been implicated as leads for the treatment of pain and a range of other disorders including neuroprotection, schizophrenia, depression and cancer.
Keywords	amino acids ; drugs ; ion channels ; neuroprotective effect ; pain ; peptides ; pharmacokinetics ; proteolysis ; receptors ; schizophrenia ; snails ; transporters ; venoms
Language	English
Dates of publication	2012-0315
Size	p. 446-455.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	204479-1
ISSN	1879-3150 ; 0041-0101
ISSN (online)	1879-3150
ISSN	0041-0101
DOI	10.1016/j.toxicon.2010.12.003
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Article ; Online: Less is More: Design of a Highly Stable Disulfide-Deleted Mutant of Analgesic Cyclic α-Conotoxin Vc1.1.

Yu, Rilei / Seymour, Victoria A L / Berecki, Géza / Jia, Xinying / Akcan, Muharrem / Adams, David J / Kaas, Quentin / Craik, David J

Scientific reports

2015 Volume 5, Page(s) 13264

Abstract: Cyclic α-conotoxin Vc1.1 (cVc1.1) is an orally active peptide with analgesic activity in rat models of neuropathic pain. It has two disulfide bonds, which can have three different connectivities, one of which is the native and active form. In this study ... ...

Abstract	Cyclic α-conotoxin Vc1.1 (cVc1.1) is an orally active peptide with analgesic activity in rat models of neuropathic pain. It has two disulfide bonds, which can have three different connectivities, one of which is the native and active form. In this study we used computational modeling and nuclear magnetic resonance to design a disulfide-deleted mutant of cVc1.1, [C2H,C8F]cVc1.1, which has a larger hydrophobic core than cVc1.1 and, potentially, additional surface salt bridge interactions. The new variant, hcVc1.1, has similar structure and serum stability to cVc1.1 and is highly stable at a wide range of pH and temperatures. Remarkably, hcVc1.1 also has similar selectivity to cVc1.1, as it inhibited recombinant human α9α10 nicotinic acetylcholine receptor-mediated currents with an IC50 of 13 μM and rat N-type (Cav2.2) and recombinant human Cav2.3 calcium channels via GABAB receptor activation, with an IC50 of ~900 pM. Compared to cVc1.1, the potency of hcVc1.1 is reduced three-fold at both analgesic targets, whereas previous attempts to replace Vc1.1 disulfide bonds by non-reducible dicarba linkages resulted in at least 30-fold decreased activity. Because it has only one disulfide bond, hcVc1.1 is not subject to disulfide bond shuffling and does not form multiple isomers during peptide synthesis.
MeSH term(s)	Amides/chemistry ; Amino Acid Sequence ; Analgesics/metabolism ; Animals ; Calcium Channels/metabolism ; Cell Line ; Conotoxins/chemistry ; Conotoxins/genetics ; Disulfides/metabolism ; Enzyme Stability ; Inhibitory Concentration 50 ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Mutation/genetics ; Oocytes/metabolism ; Protein Conformation ; Rats ; Receptors, GABA/metabolism ; Receptors, Nicotinic/metabolism ; Recombinant Proteins/chemistry ; Solutions ; Temperature ; Xenopus/metabolism
Chemical Substances	Amides ; Analgesics ; Calcium Channels ; Conotoxins ; Disulfides ; Receptors, GABA ; Receptors, Nicotinic ; Recombinant Proteins ; Solutions ; alpha-conotoxin Vc1.1 (5U5J1KR8NU)
Language	English
Publishing date	2015-08-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep13264
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Article ; Online: Engineered protease inhibitors based on sunflower trypsin inhibitor-1 (SFTI-1) provide insights into the role of sequence and conformation in Laskowski mechanism inhibition.

de Veer, Simon J / Swedberg, Joakim E / Akcan, Muharrem / Rosengren, K Johan / Brattsand, Maria / Craik, David J / Harris, Jonathan M

The Biochemical journal

2015 Volume 469, Issue 2, Page(s) 243–253

Abstract: Laskowski inhibitors regulate serine proteases by an intriguing mode of action that involves deceiving the protease into synthesizing a peptide bond. Studies exploring naturally occurring Laskowski inhibitors have uncovered several structural features ... ...

Abstract	Laskowski inhibitors regulate serine proteases by an intriguing mode of action that involves deceiving the protease into synthesizing a peptide bond. Studies exploring naturally occurring Laskowski inhibitors have uncovered several structural features that convey the inhibitor's resistance to hydrolysis and exceptional binding affinity. However, in the context of Laskowski inhibitor engineering, the way that various modifications intended to fine-tune an inhibitor's potency and selectivity impact on its association and dissociation rates remains unclear. This information is important as Laskowski inhibitors are becoming increasingly used as design templates to develop new protease inhibitors for pharmaceutical applications. In this study, we used the cyclic peptide, sunflower trypsin inhibitor-1 (SFTI-1), as a model system to explore how the inhibitor's sequence and structure relate to its binding kinetics and function. Using enzyme assays, MD simulations and NMR spectroscopy to study SFTI variants with diverse sequence and backbone modifications, we show that the geometry of the binding loop mainly influences the inhibitor's potency by modulating the association rate, such that variants lacking a favourable conformation show dramatic losses in activity. Additionally, we show that the inhibitor's sequence (including both the binding loop and its scaffolding) influences its potency and selectivity by modulating both the association and the dissociation rates. These findings provide new insights into protease inhibitor function and design that we apply by engineering novel inhibitors for classical serine proteases, trypsin and chymotrypsin and two kallikrein-related peptidases (KLK5 and KLK14) that are implicated in various cancers and skin diseases.
MeSH term(s)	Humans ; Kallikreins/antagonists & inhibitors ; Kallikreins/chemistry ; Peptides, Cyclic/chemistry ; Peptides, Cyclic/genetics ; Plant Proteins/chemistry ; Plant Proteins/genetics ; Protein Engineering ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics
Chemical Substances	Peptides, Cyclic ; Plant Proteins ; Recombinant Proteins ; SFTI-1 peptide, sunflower ; KLK14 protein, human (EC 3.4.21.-) ; KLK5 protein, human (EC 3.4.21.-) ; Kallikreins (EC 3.4.21.-)
Language	English
Publishing date	2015-07-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20150412
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Article ; Online: Cyclization of conotoxins to improve their biopharmaceutical properties.

Clark, Richard J / Akcan, Muharrem / Kaas, Quentin / Daly, Norelle L / Craik, David J

Toxicon : official journal of the International Society on Toxinology

2012 Volume 59, Issue 4, Page(s) 446–455

Abstract	Conotoxins are disulfide-rich peptides from the venoms of marine cone snails that are used in prey capture. Due to their exquisite potency and selectivity for different ion channels, receptors and transporters they have attracted much interest as leads in drug design. This article gives a brief background on conotoxins, describes their structures and highlights methods for synthetic cyclization to improve their biopharmaceutical properties. The proximity of the N and C termini of many conotoxins makes them particularly suitable for cyclization with linkers of on average five to seven amino acids. By linking the ends of conotoxins it is possible to significantly decrease their susceptibility to proteolysis without loss of their intrinsic biological activity. Here, the principles of conotoxin cyclization are illustrated with applications to the α- and χ- conotoxin classes, which have been implicated as leads for the treatment of pain and a range of other disorders including neuroprotection, schizophrenia, depression and cancer.
MeSH term(s)	Amino Acid Sequence ; Animals ; Biological Products/chemistry ; Biological Products/pharmacology ; Conotoxins/chemistry ; Cyclization ; Disulfides/chemistry ; Humans ; Ion Channels ; Molecular Sequence Data ; Protein Conformation ; Proteolysis ; Snails/chemistry
Chemical Substances	Biological Products ; Conotoxins ; Disulfides ; Ion Channels
Language	English
Publishing date	2012-03-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	204479-1
ISSN	1879-3150 ; 0041-0101
ISSN (online)	1879-3150
ISSN	0041-0101
DOI	10.1016/j.toxicon.2010.12.003
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