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Biomacromolecules. 2018; (6):1701-19
1720. DOI: 10.1021/acs.biomac.8b00
208
[199] Oppenheim FG, Xu T, McMillian
FM, Levitz SM, Diamond RD, Offner
GD, et al. Histatins a novel family of
histidine-rich proteins in human parotid
secretion isolation characterization
primary structure and fungistatic effects
on . The Journal ofCandida albicans
Biological Chemistry. 1988; (16):263
7472-7477
[200] Murakami Y, Tamagawa H,
Shizukuishi S, Tsunemitsu A, Aimoto S.
Biological role of an arginine residue
present in a histidine-rich peptide which
inhibits hemagglutination of
Porphyromonas gingivalis. FEMS
Microbiology Letters. 1992; (177 –3):201-
204. DOI: 10.1016/0378-1097(92)90156-i
[201] Burian M, Schittek B. The secrets
of dermcidin action. International
Journal of Medical Microbiology. 2015;
305(2):283-286. DOI: 10.1016/j.
ijmm.2014.12.012
[202] Muta T, Fujimoto T, Nakajima H,
Iwanaga S. Tachyplesins isolated from
hemocyte of southeast Asian horseshoe
crabs ( andCarcinoscorpius rotundicauda
Tachypleus gigas): Identification of a new
tachyplesin tachyplesin III and a
processing intermediate of its precursor.
Journal of Biochemistry. 1990; (9):108
261-266. DOI: 10.1093/oxfordjournals.
jbchem.a123191
[203] Liu C, Qi J, Shan B, Ma Y.
Tachyplesin causes membrane
instability that kills multidrug-resistant
bacteria by inhibiting the 3-ketoacyl
carrier protein reductase FabG.
Frontiers in Microbiology. 2018; :825.9
DOI: 10.3389/fmicb.2018.00825
[204] Rahbar MR, Zarei M, Jahangiri A,
Khalili S, Nezafat N, Negahdaripour M,
et al. Pierce into the native structure of
Ata, a trimeric autotransporter of
Acinetobacter baumannii ATCC 17978.
Int. J. Pept. Res. Therapeut. 2020; :26
1269-1282
[205] Jahangiri A, Rasooli I, Owlia P,
Fooladi AAI, Salimian J. An integrative
in silico approach to the structure of
Omp33-36 in .Acinetobacter baumannii
Computational Biology and Chemistry.
2018; :77-86. DOI: 10.1016/j.72
compbiolchem.2018.01.003
[206] Rasooli I, Abdolhamidi R, Jahangiri
A, Astaneh DAS. Outer membrane
protein Oma87 prevents Acinetobacter
baumannii infection. International
Journal of Peptide Research and
Therapeutics. 2020; :1-8. DOI: 10.1007/9
s10989-020-10056-0
[207] Rahbar MR, Zarei M, Jahangiri A,
Khalili S, Nezafat N, Negahdaripour M,
et al. Trimeric autotransporter adhesins
in coincidentalAcinetobacter baumannii
evolution at work. Infection, Genetics
and Evolution. 2019; :116-127. DOI:71
10.1016/j. meegid.2019.03.023
[208] Nagarajan D, Nagarajan T, Roy N,
Kulkarni O, Ravichandran S, Mishra M,
et al. The Journal of Biological
Chemistry. 2018; (10):3492-3509.293
DOI: 10.1074/jbc.M117.805499
[209] Misawa T, Goto C, Shibata N,
Hirano M, Kikuchi Y, Naito M, et al.
Rationaldesign of novel amphipathic
antimicrobial peptides focused on the
distribution of cationic amino acid
residues. Med. Chem. Comm. 2019;10(6):
896-900. DOI: 10.1039/c9md0 0166b
[210] Khan MTH. Recent Trends on
QSAR in the Pharmaceutical
Perceptions. Sharjah, United Arab
Emirates: Bentham Science Publishers;
2012. ISBN: 978-1-60805-433-6
[211] Wu X, Wang Z, Li X, Fan Y, He G,
Wan Y, et al. In vitro and in vivo
activities of antimicrobial peptides
developed using an amino acid-based
activity prediction method.
Antimicrobial Agents and
Insights on Antimicrobial Peptides
151
https://t.me/medicina_free
Chemotherapy. 2014; (9):58
5342-5349
[212] Ageitos JM, Sánchez-Pérez A, Calo-
Mata P, Villa TG. Antimicrobial
peptides (AMPs): Ancient compounds
that represent novel weapons in the
fight against bacteria. Biochemical
Pharmacology. 2017; :117. DOI:133
10.1016/j.bcp.2016.09.018
[213] Andersson DI, Hughes D, Kubicek-
Sutherland JZ. Mechanisms and
consequences of bacterial resistance to
antimicrobial peptides. Drug Resistance
Updates. 2016; :43-57. DOI: 10.1016/26
j.drup. 2016.04.002
[214] MoravejH, Moravej Z, Yazdanparast
M, Heiat M, Mirhosseini A, Moghaddam
MM, et al. Antimicrobial peptides:
Features action and their resistance
mechanismsin bacteria. Microbial Drug
Resistance. 2018;24(6):747. DOI: 10.1089/
mdr.2017.0392
[215] Joo HS, Fu CI, Otto M. Bacterial
strategies of resistance to antimicrobial
peptides. Phil. Trans. R. Soc. Lond. B.
Biol. Sci. 2016; (1695):20150292. DOI:371
10.1098/rstb. 2015.0292
[216] Omardien S, Brul S, Zaat SAJ.
Antimicrobial activity of cationic
antimicrobial peptides against gram-
positive: Current progress made in
understanding the mode of action and
the response of bacteria. Front. Cell.
Develop. Biol. 2016; :111. DOI: 10.3389/4
fcell.2016.00111
[217] Jeannot K, Bolard A, Plésiat P.
Resistance to polymyxins in gram-
negative organisms. Int. J. Antimicr Ag.
2017; (5):526-535. DOI: 10.1016/j.49
ijantimicag.2016. 11.029
[218] Liu YY, Wang Y, Walsh TR, Yi LX,
Zhang R, Spencer J, et al. Emergence of
plasmid-mediated colistin resistance
mechanism MCR-1 in animals and
human beings in China: A
microbiological and molecular biological
study. The Lancet Infectious Diseases.
2016; (2):161-168. DOI: 10.1016/16
S1473-3099(15)00424-7
[219] Paterson DL, Harris PNA. Colistin
resistance: A major breach in our last
line of defense. The Lancet Infectious
Diseases. 2016; (2):132-133. DOI:16
10.1016/S1473-3099(15)00463-6
[220] Macnair CR, Stokes JM, Carfrae
LA, Fiebig-Comyn AA, Coombes BK,
Mulvey MR, et al. Overcoming mcr-1
mediated colistin resistance with colistin
in combination with other antibiotics.
Nature Communications. 2018; (1):458.9
DOI: 10.1038/s41467-018-02875-z
[221] Morita Y, Tomida J, Kawamura Y.
MexXY multidrug efflux system of
Pseudomonas aeruginosa. Frontiers in
Microbiology. 2012; :408. DOI: 10.3389/3
fmicb.2012.00408
[222] Bechinger B, Gorr SU.
Antimicrobial peptides: Mechanisms of
action and resistance. Journal of Dental
Research. 2017; (3):254-260. DOI:96
10.1177/0022034516679973
[223] Gheorghe I, Saviuc C, Ciubuca B,
Lazar V, Chifiriuc MC. Chapter 8—Nano
drug delivery. In: Grumezescu AM,
editor. Nanomaterials for Drug Delivery
and Therapy. Norwich NY USA:William
Andrew Publishing; 2019. pp. 225-244.
ISBN: 978-0-12-816505-8
[224] Sun B, Wibowo D, Middelberg
APJ, Zhao CX. Cost-effective
recombinantly produced pexiganan
peptide and its antimicrobial activity.
AMB Express. 2018; (1):1-14. DOI:8
10.1186/s13568-018-0541-3
[225] Brannon JR, Burk DL, Leclerc JM,
Thomassin JL, Portt A, Berghuis AM,
et al. Inhibition of outer membrane
proteases of the omptin family by
aprotinin. Infection and Immunity.
2015; (6):2300-2311. DOI: 10.1128/83
IAI.00136-15
Peptides with Therapeutic Potential against InfectionsAcinetobacter baumanii
DOI: http://dx.doi.org/10.5772/ TexLi.1I 00389
152
https://t.me/medicina_free
Peptides with Therapeutic Potential against Acinetobacter baumanii Infectionsc
153
https://t.me/medicina_free
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