β-折叠抗菌肽的研发及应用策略

doi:10.11843/j.issn.0366-6964.2022.08.008

Abstract

Abstract: The abuse of antibiotics has led to the problem of bacterial resistance more and more serious in the world, which has posed a great threat to the health of human beings and livestock as well as the development of animal husbandry. Antimicrobial peptides (AMPs), which have diverse functions and are not tend to cause bacterial resistance, have gradually developed into potential substitutes of antibiotics. β-sheet structure is a major secondary element constituting the classification of AMPs, which usually maintains the structural stability through one or more disulfide bonds. Compared with the widely studied α-helical AMP, they are believed to have stronger resistance to enzymolysis and higher cell selectivity. This review briefly introduces the natural sources and antibacterial mechanism of β-sheet AMPs, and sorts out some common molecular design methods and application strategies. The content obtained here can provide novel ideas for the research and application of β-sheet AMPs.

Key words: β-sheet antimicrobial peptides, molecular design, antibacterial mechanism, application strategy

CLC Number:

SHAO Changxuan, DANG Ankai, ZHAN Zhaohan, LAI Zhenheng, ZHU Yongjie, SHAN Anshan. Development and Application Strategy of Beta Sheet Antimicrobial Peptides[J]. Acta Veterinaria et Zootechnica Sinica, 2022, 53(8): 2490-2501.

References 82

[1]	SCOTT H M, ACUFF G, BERGERON G, et al. Critically important antibiotics:criteria and approaches for measuring and reducing their use in food animal agriculture[J]. Ann N Y Acad Sci, 2019, 1441(1):8-16.
[2]	雷龙, 周颖, 李俊杰, 等. 从欧盟禁抗看国内无抗的趋势[J]. 广东饲料, 2020, 29(10):11-14.LEI L, ZHOU Y, LI J J, et al. Looking at the trend of domestic non-resistance from the EU's anti-resistance ban[J]. Guangdong Feed, 2020, 29(10):11-14. (in Chinese)
[3]	李静. 抗菌肽的生物学特性及在畜禽养殖中的应用[J]. 现代畜牧科技, 2021(9):23-24.LI J. Biological functions of antimicrobial peptides and its application in livestock and poultry breeding[J]. Modern Animal Husbandry Science & Technology, 2021(9):23-24. (in Chinese)
[4]	MAHLAPUU M, BJÖRN C, EKBLOM J. Antimicrobial peptides as therapeutic agents:opportunities and challenges[J]. Crit Rev Biotechnol, 2020, 40(7):978-992.
[5]	SHAO C X, ZHU Y J, LAI Z H, et al. Antimicrobial peptides with protease stability:progress and perspective[J]. Future Med Chem, 2019, 11(16):2047-2050.
[6]	WANG G S. Improved methods for classification, prediction, and design of antimicrobial peptides[M]//ZHOU P, HUANG J. Computational Peptidology. New York:Humana Press, 2015:43-66.
[7]	KOEHBACH J, CRAIK D J. The vast structural diversity of antimicrobial peptides[J]. Trends Pharmacol Sci, 2019, 40(7):517-528.
[8]	巫春旭, 卢雪梅, 金小宝, 等.天蚕素类抗菌肽分子设计研究进展[J]. 中国生物工程杂志, 2016, 36(2):96-100.WU C X, LU X M, JIN X B, et al. Advances in research on molecular design of cecropin-like peptides[J]. China Biotechnology, 2016, 36(2):96-100. (in Chinese)
[9]	AMOS S B T A, VERMEER L S, FERGUSON P M, et al. Antimicrobial peptide potency is facilitated by greater conformational flexibility when binding to gram-negative bacterial inner membranes[J]. Sci Rep, 2016, 6(1):37639.
[10]	WANG C K, CRAIK D J. Designing macrocyclic disulfide-rich peptides for biotechnological applications[J]. Nat Chem Biol, 2018, 14(5):417-427.
[11]	WANG J J, DOU X J, SONG J, et al. Antimicrobial peptides:promising alternatives in the post feeding antibiotic era[J]. Med Res Rev, 2019, 39(3):831-859.
[12]	BASTOS P, TRINDADE F, DA COSTA J, et al. Human antimicrobial peptides in bodily fluids:current knowledge and therapeutic perspectives in the postantibiotic era[J]. Med Res Rev, 2018, 38(1):101-146.
[13]	TORRES A M, KUCHEL P W. The β-defensin-fold family of polypeptides[J]. Toxicon, 2004, 44(6):581-588.
[14]	POWERS J P S, HANCOCK R E W. The relationship between peptide structure and antibacterial activity[J]. Peptides, 2003, 24(11):1681-1691.
[15]	LEE J H, SHIN S M. Understanding β-hairpin formation:computational studies for three different hairpins[J]. Bull Korean Chem Soc, 2008, 29(4):741-748.
[16]	PANTELEEV P V, BALANDIN S V, IVANOV V T, et al. A therapeutic potential of animal β-hairpin antimicrobial peptides[J]. Curr Med Chem, 2017, 24(17):1724-1746.
[17]	SHAFEE T M A, LAY F T, PHAN T K, et al. Convergent evolution of defensin sequence, structure and function[J]. Cell Mol Life Sci, 2017, 74(4):663-682.
[18]	GAO X H, DING J Q, LIAO C B, et al. Defensins:the natural peptide antibiotic[J]. Adv Drug Deliv Rev, 2021, 179:114008.
[19]	ANDERSSON H S, FIGUEREDO S M, HAUGAARD-KEDSTRÖM L M, et al. The α-defensin salt-bridge induces backbone stability to facilitate folding and confer proteolytic resistance[J]. Amino Acids, 2012, 43(4):1471-1483.
[20]	HOSSAIN F, MOGHAL M R, ISLAM Z, et al. Membrane potential is vital for rapid permeabilization of plasma membranes and lipid bilayers by the antimicrobial peptide lactoferricin B Membrane potential is vital for AMP-induced permeabilization[J]. J Biol Chem, 2019, 294(27):10449-10462.
[21]	FEHLBAUM P, BULET P, CHERNYSH S, et al. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides[J]. Proc Natl Acad Sci U S A, 1996, 93(3):1221-1225.
[22]	SELSTED M E, HARWIG S S, GANZ T, et al. Primary structures of three human neutrophil defensins[J]. J Clin Invest, 1985, 76(4):1436-1439.
[23]	DE LEEUW E, BURKS S R, LI X Q, et al. Structure-dependent functional properties of human defensin 5[J]. FEBS Lett, 2007, 581(3):515-520.
[24]	SILVA P I JR, DAFFRE S, BULET P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family[J]. J Biol Chem, 2000, 275(43):33464-33470.
[25]	PARK C H, VALORE E V, WARING A J, et al. Hepcidin, a urinary antimicrobial peptide synthesized in the liver[J]. J Biol Chem, 2001, 276(11):7806-7810.
[26]	施益如, 李暄, 蔡明烩, 等. 抗菌肽Protegrin-1的研究进展[J]. 中国畜牧杂志, 2021, 57(6):67-72.SHI Y R, LI X, CAI M H, et al. Research progress on antimicrobial peptide protegrin-1[J]. Chinese Journal of Animal Science, 2021, 57(6):67-72. (in Chinese)
[27]	NAKAMURA T, FURUNAKA H, MIYATA T, et al. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure[J]. J Biol Chem, 1988, 263(32):16709-16713.
[28]	HUBER A, GALGÓCZY L, VÁRADI G, et al. Two small, cysteine-rich and cationic antifungal proteins from Penicillium chrysogenum:a comparative study of PAF and PAFB[J]. Biochim Biophys Acta Biomembr, 2020, 1862(8):183246.
[29]	PAVITHRRA G, RAJASEKARAN R. Gramicidin peptide to combat antibiotic resistance:a review[J]. Int J Pept Res Ther, 2020, 26(1):191-199.
[30]	WANG G S. Human antimicrobial peptides and proteins[J]. Pharmaceuticals (Basel, Switzerland), 2014, 7(5):545-594.
[31]	WANG Q, REN M J, LIU X Y, et al. Peptidoglycan recognition proteins in insect immunity[J]. Mol Immunol, 2019, 106:69-76.
[32]	WANG Y P, LAI R. Insect antimicrobial peptides:structures, properties and gene regulation[J]. Dongwuxue Yanjiu, 2010, 31(1):27-34.
[33]	BARBAULT F, LANDON C, GUENNEUGUES M, et al. Solution structure of Alo-3:a new knottin-type antifungal peptide from the insect Acrocinus longimanus[J]. Biochemistry, 2003, 42(49):14434-14442.
[34]	ISOZUMI N, MASUBUCHI Y, IMAMURA T, et al. Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula[J]. Sci Rep, 2021, 11(1):9923.
[35]	TAM J P, WANG S J, WONG K H, et al. Antimicrobial peptides from plants[J]. Pharmaceuticals (Basel, Switzerland), 2015, 8(4):711-757.
[36]	陈鹏. 细菌素在动物饲料中的替抗应用[J]. 饲料研究, 2021, 44(18):150-153.CHEN P. Antibiotic replacement application of bacteriocins in animal feed[J]. Feed Research, 2021, 44(18):150-153. (in Chinese)
[37]	BROGDEN K A. Antimicrobial peptides:pore formers or metabolic inhibitors in bacteria?[J]. Nat Rev Microbiol, 2005, 3(3):238-250.
[38]	MOOKHERJEE N, ANDERSON M A, HAAGSMAN H P, et al. Antimicrobial host defence peptides:functions and clinical potential[J]. Nat Rev Drug Discov, 2020, 19(5):311-332.
[39]	LI S Q, WANG Y J, XUE Z H, et al. The structure-mechanism relationship and mode of actions of antimicrobial peptides:A review[J]. Trends Food Sci Technol, 2021, 109:103-115.
[40]	张溪, 弓磊. 抗菌肽抗菌机制及研究热点[J]. 中国组织工程研究, 2020, 24(10):1634-1640.ZHANG X, GONG L. Antimicrobial mechanism of antimicrobial peptide and research progress[J]. Chinese Journal of Tissue Engineering Research, 2020, 24(10):1634-1640. (in Chinese)
[41]	BELLAMY W, TAKASE M, WAKABAYASHI H, et al. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin[J]. J Appl Bacteriol, 1992, 73(6):472-479.
[42]	SINHA S, NG W J, BHATTACHARJYA S. NMR structure and localization of the host defense antimicrobial peptide thanatin in zwitterionic dodecylphosphocholine micelle:Implications in antimicrobial activity[J]. Biochim Biophys Acta Biomembr, 2020, 1862(11):183432.
[43]	MANI R, CADY S D, TANG M, et al. Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR[J]. Proc Natl Acad Sci U S A, 2006, 103(44):16242-16247.
[44]	JENSSEN H, HAMILL P, HANCOCK R E W. Peptide antimicrobial agents[J]. Clin Microbiol Rev, 2006, 19(3):491-511.
[45]	DE LEEUW E, LI C Q, ZENG P Y, et al. Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II[J]. FEBS Lett, 2010, 584(8):1543-1548.
[46]	CHO J, LEE D G. The antimicrobial peptide arenicin-1 promotes generation of reactive oxygen species and induction of apoptosis[J]. Biochim Biophys Acta Gen Subj, 2011, 1810(12):1246-1251.
[47]	OVCHINNIKOVA T V, ALESHINA G M, BALANDIN S V, et al. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina[J]. FEBS Lett, 2004, 577(1-2):209-214.
[48]	SHAH P, CHEN C S. Systematical screening of intracellular protein targets of polyphemusin-I using Escherichia coli proteome microarrays[J]. Int J Mol Sci, 2021, 22(17):9158.
[49]	ZHAN J, JIA H S, SEMCHENKO E A, et al. Self-derived structure-disrupting peptides targeting methionine aminopeptidase in pathogenic bacteria:a new strategy to generate antimicrobial peptides[J]. FASEB J, 2019, 33(2):2095-2104.
[50]	SONG J, WANG J J, ZHAN N, et al. Therapeutic potential of trp-rich engineered amphiphiles by single hydrophobic amino acid end-tagging[J]. ACS Appl Mater Interfaces, 2019, 11(47):43820-43834.
[51]	TAKAHASHI D, SHUKLA S K, PRAKASH O, et al. Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity[J]. Biochimie, 2010, 92(9):1236-1241.
[52]	BENFIELD A H, DEFAUS S, LAWRENCE N, et al. Cyclic gomesin, a stable redesigned spider peptide able to enter cancer cells[J]. Biochim Biophys Acta Biomembr, 2021, 1863(1):183480.
[53]	DONG N, ZHU X, CHOU S, et al. Antimicrobial potency and selectivity of simplified symmetric-end peptides[J]. Biomaterials, 2014, 35(27):8028-8039.
[54]	VINEETHKUMAR T V, ASHA R, SHYLA G, et al. Post-translationally modified frog skin-derived antimicrobial peptides are effective against Aeromonas sobria[J]. Microb Pathog, 2017, 104:287-288.
[55]	GOMES B, AUGUSTO M T, FELÍCIO M R, et al. Designing improved active peptides for therapeutic approaches against infectious diseases[J]. Biotechnol Adv, 2018, 36(2):415-429.
[56]	LEI R Y, HOU J C, CHEN Q X, et al. Self-assembling myristoylated human α-defensin 5 as a next-generation nanobiotics potentiates therapeutic efficacy in bacterial infection[J]. ACS Nano, 2018, 12(6):5284-5296.
[57]	IMURA Y, NISHIDA M, OGAWA Y, et al. Action mechanism of tachyplesin I and effects of PEGylation[J]. Biochim Biophys Acta Biomembr, 2007, 1768(5):1160-1169.
[58]	CHAN L Y, ZHANG V M, HUANG Y H, et al. Cyclization of the antimicrobial peptide gomesin with native chemical ligation:influences on stability and bioactivity[J]. ChemBioChem, 2013, 14(5):617-624.
[59]	FOX M A, THWAITE J E, ULAETO D O, et al. Design and characterization of novel hybrid antimicrobial peptides based on cecropin A, LL-37 and magainin II[J]. Peptides, 2012, 33(2):197-205.
[60]	BALABAN N, GOV Y, GIACOMETTI A, et al. A chimeric peptide composed of a dermaseptin derivative and an RNA III-inhibiting peptide prevents graft-associated infections by antibiotic-resistant staphylococci[J]. Antimicrob Agents Chemother, 2004, 48(7):2544-2550.
[61]	LIU Y F, XIA X, XU L, et al. Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity[J]. Biomaterials, 2013, 34(1):237-250.
[62]	TORRES M D T, SOTHISELVAM S, LU T K, et al. Peptide design principles for antimicrobial applications[J]. J Mol Biol, 2019, 431(18):3547-3567.
[63]	SHAO C X, ZHU Y J, JIAN Q, et al. Cross-strand interaction, central bending, and sequence pattern act as biomodulators of simplified β-hairpin antimicrobial amphiphiles[J]. Small, 2021, 17(7):2003899.
[64]	WU H, ONG Z Y, LIU S Q, et al. Synthetic β-sheet forming peptide amphiphiles for treatment of fungal keratitis[J]. Biomaterials, 2015, 43:44-49.
[65]	CHOU S, WANG J J, SHANG L, et al. Short, symmetric-helical peptides have narrow-spectrum activity with low resistance potential and high selectivity[J]. Biomater Sci, 2019, 7(6):2394-2409.
[66]	HAMMAMI R, FLISS I. Current trends in antimicrobial agent research:chemo- and bioinformatics approaches[J]. Drug Discovery Today, 2010, 15(13-14):540-546.
[67]	CHERKASOV A, HILPERT K, JENSSEN H, et al. Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs[J]. ACS Chem Biol, 2009, 4(1):65-74.
[68]	FJELL C D, JENSSEN H, CHEUNG W A, et al. Optimization of antibacterial peptides by genetic algorithms and cheminformatics[J]. Chem Biol Drug Des, 2011, 77(1):48-56.
[69]	李丘轲, 李金泽, 吴华, 等. 靶向抗菌肽的设计策略与应用[J]. 畜牧兽医学报, 2020, 51(2):243-251.LI Q K, LI J Z, WU H, et al. Design strategy and application on targeted antimicrobial peptides[J]. Acta Veterinaria et Zootechnica Sinica, 2020, 51(2):243-251. (in Chinese)
[70]	邓赣奇, 黄增颖, 梁耀文, 等. "减抗"、"替抗"背景下抗菌肽的应用和研究进展[J]. 家畜生态学报, 2020, 41(6):1-7.DENG G Q, HUANG Z Y, LIANG Y W, et al. Application and research advance of antimicrobial peptide[J]. Acta Ecologiae Animalis Domastici, 2020, 41(6):1-7. (in Chinese)
[71]	ECKERT R, QI F X, YARBROUGH D K, et al. Adding selectivity to antimicrobial peptides:rational design of a multidomain peptide against Pseudomonas spp[J]. Antimicrob Agents Chemother, 2006, 50(4):1480-1488.
[72]	URBAN P, VALLE-DELGADO J J, MOLES E, et al. Nanotools for the delivery of antimicrobial peptides[J]. Curr Drug Targets, 2012, 13(9):1158-1172.
[73]	PARDHI D M, KARAMAN D ?瘙塁, TIMONEN J, et al. Anti-bacterial activity of inorganic nanomaterials and their antimicrobial peptide conjugates against resistant and non-resistant pathogens[J]. Int J Pharm, 2020, 586:119531.
[74]	SOUSA M G C, REZENDE T M B, FRANCO O L. Nanofibers as drug-delivery systems for antimicrobial peptides[J]. Drug Discov Today, 2021, 26(8):2064-2074.
[75]	康芷若, 王如霞, 陈梦涵, 等. 纳米材料作为抗菌肽递送载体的研究进展[J]. 动物医学进展, 2021, 42(6):97-102.KANG Z R, WANG R X, CHEN M H, et al. Progress on nanomaterials as vehicles for delivery of antimicrobial peptides[J]. Progress in Veterinary Medicine, 2021, 42(6):97-102. (in Chinese)
[76]	STOLNIK S, ILLUM L, DAVIS S S. Long circulating microparticulate drug carriers[J]. Adv Drug Deliv Rev, 2012, 64:290-301.
[77]	GERA S, KANKURI E, KOGERMANN K. Antimicrobial peptides-unleashing their therapeutic potential using nanotechnology[J]. Pharmacol Ther, 2022, 232:107990.
[78]	TEIXEIRA M C, CARBONE C, SOUSA M C, et al. Nanomedicines for the delivery of antimicrobial peptides (AMPs)[J]. Nanomaterials (Basel), 2020, 10(3):560.
[79]	HANEY E F, HUNTER H N, MATSUZAKI K, et al. Solution NMR studies of amphibian antimicrobial peptides:linking structure to function?[J]. Biochim Biophys Acta Biomembr, 2009, 1788(8):1639-1655.
[80]	LAZZARO B P, ZASLOFF M, ROLFF J. Antimicrobial peptides:application informed by evolution[J]. Science, 2020, 368(6490):eaau5480.
[81]	KIM J M, JANG S J, YANG M H, et al. Characterization of antibacterial activity and synergistic effect of cationic antibacterial peptide-resin conjugates[J]. Bull Korean Chem Soc, 2011, 32(11):3928-3932.
[82]	刘又铭, 房鑫, 陈璐, 等. 牛乳源肽Lfcin B抗菌活性、稳定性及协同效应研究[J]. 饲料工业, 2021, 42(3):49-53.LIU Y M, FANG X, CHEN L, et al. Study on antibacterial activity, stability and synergistic effect of Lactoferricin Bovine[J]. Feed Industry, 2021, 42(3):49-53. (in Chinese)

Development and Application Strategy of Beta Sheet Antimicrobial Peptides

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