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{{short description|Chemical compound}}
]
{{cs1 config|name-list-style=vanc}}
] groups on the ] as well as ] of select amide nitrogens to force cyclic conformation. <ref>{{citation | title =Stereochemistry of Protected Ornithine Side Chains of Gramicidin S Derivatives: X-ray Crystal Structure of the Bis-Boc-tetra-N-methyl Derivative of Gramicidin S |first = Keiichi Yamada, Masafumi Unno, Kyoko Kobayashi, Hiroyuki Oku, Hatsuo Yamamura, Shuki Araki, Hideyuki Matsumoto, Ryoichi Katakai, and Masao Kawai
{{Drugbox
| journal = J. Am. Chem. Soc.; | year = 2002; | issue = 124 |page = 12684 - 12688; | DOI = 10.1021/ja020307t }}</ref>]] '''Gramicidin S''' is a derivative of ], produced by the ] bacterium ''Bacillus brevis var. G.-B''. Gramicidin S is a ], constructed as two identical ]s joined head to tail, formally written as ''cyclo''(-]-]-]-D-]-]-)<sub>2</sub>. That is to say, it forms a ring structure composed of five different amino acids, each one used twice within the structure. Another interesting point is that it utilizes two amino acids uncommon in ]: ] as well as the unnatural ] of ]. It is synthesized by gramicidin S synthetase.<ref>
| verifiedrevid = 443848998
{{Citation | last = Brick | first = Peter | author-link = Peter Brike | title = Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S | journal = The EMBO Journal | volume = 16 | pages = 4174-4183 | date = 1997 | year = 1997 | DOI = 10.1093/emboj/16.14.4174 }}</ref> Structurally, Gramicidin S differs from ], which is a linear ] and forms a beta helix in ]s. The exact mechanism by which Gramicidin S works is not well known.
| IUPAC_name = Gramicidin S
| image = Gramicidin S.svg
| alt = Structural formula of Gramicidin S
| image2 = Gramicidin S 3D ball.png
| alt2 = Ball-and-stick model of the Gramicidin S molecule
| width = 260


<!--Clinical data-->
It has a ] of ca. 1,300 and is a transparent yellow or light yellow liquid and is usually encapsulated in two-percent sterile spirit solution. First used in 1943 by ] during ] (thus is also known as Gramicidin S). It also exists in the form of pills (Latin: ''tabulettae Gramicidini'') and paste (''pasta Gramicidini''). The last could be also used as a ], being introduced into vagina by the special syringe.{{Fact|date=July 2007}}
| tradename =
⚫ ==References==
| pregnancy_AU = <!-- A / B1 / B2 / B3 / C / D / X -->
<references />
| pregnancy_US = <!-- A / B / C / D / X -->
| legal_AU = <!-- Unscheduled / S2 / S4 / S8 -->
| legal_UK = <!-- GSL / P / POM / CD -->
| legal_US = <!-- OTC / Rx-only -->
| routes_of_administration = Topical


<!--Identifiers-->
⚫ ]
| CAS_number_Ref = {{cascite|correct|??}}
| CAS_number = 113-73-5
| UNII_Ref = {{fdacite|correct|FDA}}
| UNII = WHM29QA23F
| PubChem = 73357
| DrugBank_Ref = {{drugbankcite|correct|drugbank}}
| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID = 66085
| NIAID_ChemDB = 002002
| ChEBI_Ref = {{ebicite|correct|EBI}}
| ChEBI = 5530
| ChEMBL_Ref = {{ebicite|correct|EBI}}
| ChEMBL = 373496


<!--Chemical data-->
{{protein-stub}}
| C=60 | H=92 | N=12 | O=10
| smiles = CC(C)C1C(=O)N(C(=O)N2CCC2C(=O)N(C(=O)N(C(=O)N(C(=O)N(C(=O)N3CCC3C(=O)N(C(=O)N(C(=O)N1)CCCN)C(C)C)Cc4ccccc4)CC(C)C)CCCN)C(C)C)Cc5ccccc5
| StdInChI_Ref = {{stdinchicite|correct|chemspider}}
| StdInChI = 1S/C60H92N12O10/c1-35(2)31-43-53(75)67-45(33-39-19-11-9-12-20-39)59(81)71-29-17-25-47(71)55(77)70-50(38(7)8)58(80)64-42(24-16-28-62)52(74)66-44(32-36(3)4)54(76)68-46(34-40-21-13-10-14-22-40)60(82)72-30-18-26-48(72)56(78)69-49(37(5)6)57(79)63-41(23-15-27-61)51(73)65-43/h9-14,19-22,35-38,41-50H,15-18,23-34,61-62H2,1-8H3,(H,63,79)(H,64,80)(H,65,73)(H,66,74)(H,67,75)(H,68,76)(H,69,78)(H,70,77)/t41-,42-,43-,44-,45+,46+,47-,48-,49-,50-/m0/s1
| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}
| StdInChIKey = IUAYMJGZBVDSGL-XNNAEKOYSA-N
}}
'''Gramicidin S''' or '''Gramicidin Soviet'''<ref>{{cite journal | vauthors = Gause GF, Brazhnikova MG | s2cid = 4125407 | doi = 10.1038/154703a0 | title = Gramicidin S and its use in the Treatment of Infected Wounds | year = 1944 | pages = 703 | volume = 154 | journal = ] | issue=3918| bibcode = 1944Natur.154..703G | doi-access = free }}</ref> is an antibiotic that is effective against some ] and ] as well as some ].

It is a derivative of ], produced by the gram-positive bacterium '']''. Gramicidin S is a cyclodecapeptide, constructed as two identical ] joined head to tail, formally written as ''cyclo''(-]-]-]-D-]-]-)<sub>2</sub>. That is to say, it forms a ring structure composed of five different amino acids, each one used twice within the structure.<ref>{{cite journal | vauthors = Llamas-Saiz AL, Grotenbreg GM, Overhand M, van Raaij MJ | title = Double-stranded helical twisted beta-sheet channels in crystals of gramicidin S grown in the presence of trifluoroacetic and hydrochloric acids | journal = Acta Crystallographica. Section D, Biological Crystallography | volume = 63 | issue = Pt 3 | pages = 401–7 | date = March 2007 | pmid = 17327677 | doi = 10.1107/S0907444906056435 | bibcode = 2007AcCrD..63..401L }}</ref> Another interesting point is that it utilizes two amino acids uncommon in ]s: ] as well as the atypical ] of ]. It is synthesized by gramicidin S synthetase.<ref>{{cite journal | vauthors = Conti E, Stachelhaus T, Marahiel MA, Brick P | title = Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S | journal = The EMBO Journal | volume = 16 | issue = 14 | pages = 4174–83 | date = July 1997 | pmid = 9250661 | pmc = 1170043 | doi = 10.1093/emboj/16.14.4174 }}</ref>

== Biosynthesis ==

Gramicidin S biosynthetic pathway consists of two-enzyme of nonribosomal peptide synthases (]), gramicidin S synthetase I (GrsA) and gramicidin S synthetase II (GrsB), to give a product as a cyclic decapeptide. Within the biosynthetic pathway, there are total of five modules that specifically recognize, activate, and condense the amino acids to gramicidin S. Starting module GrsA consists of three domains: Adenylation (A) domain where it incorporates the amino acid and activates it by adenylation using ATP, Thiolation (T) domain or peptidyl carrier protein (PCP) in which the adenylated amino acid gets covalently attached to the 4´-phosphopantetheine group and this gets loaded onto the conserved serine in the T domain, Epimerization (E) domain where it epimerizes L-amino acid to D-amino acid.<ref name="pmid7534306">{{cite journal | vauthors = Stachelhaus T, Marahiel MA | s2cid = 10325408 | title = Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA | journal = The Journal of Biological Chemistry | volume = 270 | issue = 11 | pages = 6163–9 | date = March 1995 | pmid = 7534306 | doi = 10.1074/jbc.270.11.6163 | doi-access = free }}</ref><ref name="pmid11851477">{{cite journal | vauthors = von Döhren H, Keller U, Vater J, Zocher R | title = Multifunctional Peptide Synthetases | journal = Chemical Reviews | volume = 97 | issue = 7 | pages = 2675–2706 | date = November 1997 | pmid = 11851477 | doi = 10.1021/cr9600262 }}</ref><ref name="pmid15700962">{{cite journal | vauthors = Sieber SA, Marahiel MA | title = Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics | journal = Chemical Reviews | volume = 105 | issue = 2 | pages = 715–38 | date = February 2005 | pmid = 15700962 | doi = 10.1021/cr0301191 }}</ref> Starting module GrsA loads D-Phe onto the system.{{cn|date=February 2023}}

Second enzyme cluster GrsB contains four ], each containing condensation (C), adenylation (A), and thiolation (T) domains and ] domain (TE) at the end. C domain forms a peptide bond between two amino acids, D-Phe and L-Pro. L-Val, L-Orn, and L-Leu are incorporated sequentially by the next three modules of GrsB. After repeating the whole module synthesis once again, TE domain cyclizes and releases the two peptides and dimerize them together to form the final product.<ref name="pmid16195555">{{cite journal | vauthors = Miller LM, Mazur MT, McLoughlin SM, Kelleher NL | title = Parallel interrogation of covalent intermediates in the biosynthesis of gramicidin S using high-resolution mass spectrometry | journal = Protein Science | volume = 14 | issue = 10 | pages = 2702–12 | date = October 2005 | pmid = 16195555 | pmc = 2253301 | doi = 10.1110/ps.051553705 }}</ref>

]

== History ==
Gramicidin S was discovered by Russian microbiologist ] and his wife Maria Brazhnikova in 1942. Within the year Gramicidin S was being used in Soviet military hospitals to treat infection and eventually found usage at the front lines of combat by 1946.<ref name="pmid12212443">{{cite journal | vauthors = Gall YM, Konashev MB | title = The discovery of Gramicidin S: the intellectual transformation of G.F. Gause from biologist to researcher of antibiotics and on its meaning for the fate of Russian genetics | journal = History and Philosophy of the Life Sciences | volume = 23 | issue = 1 | pages = 137–50 | year = 2001 | pmid = 12212443 }}</ref> Gause was awarded the ] for Medicine for his discovery in 1946. In 1944, Gramicidin S was sent by the ] to ] via the ] in a collaborative effort to establish the exact structure. English chemist ] proved that the compound was an original antibiotic and a polypeptide using paper chromatography.<ref>{{cite encyclopedia | url = http://www.britannica.com/eb/article-9070753/RLM-Synge | title = R.L.M. Synge (British biochemist) | encyclopedia = Britannica Online Encyclopedia | date = 24 October 2023 }}</ref> He would later go on to receive the ] for his work in chromatography. The crystal structure was finally established by ] and ]; ] worked for a term in 1947 with Gerhard Schmidt on the antibiotic Gramicidin S, as an undergraduate research project. The importance of Gramicidin S and antibiotic research in general was so great that Gause was not persecuted during the period of ] in the USSR, while many of his colleagues were. Indeed, it was his need for developing new strains to mass-produce antibiotics that allowed politically sanctioned collaborations with ]s like Joseph Rapoport and Alexander Malinovsky, who would both actively participate in the downfall of Lysenkoism.<ref name="pmid12212443" />

== Structure and pharmacological effect ==
] on the ] as well as ] of select amide nitrogens to force cyclic conformation.<ref>{{cite journal | vauthors = Yamada K, Unno M, Kobayashi K, Oku H, Yamamura H, Araki S, Matsumoto H, Katakai R, Kawai M | display-authors = 6 | title = Stereochemistry of protected ornithine side chains of gramicidin S derivatives: X-ray crystal structure of the bis-Boc-tetra-N-methyl derivative of gramicidin S | journal = Journal of the American Chemical Society | volume = 124 | issue = 43 | pages = 12684–8 | date = October 2002 | pmid = 12392415 | doi = 10.1021/ja020307t }}</ref>]]

Gramicidin S differs from other gramicidin types in that it is a cationic cyclic decapeptide and has a structure of an anti-parallel beta-sheet. Gramicidin S molecule is ], with hydrophobic amino acids (D-Phe, Val, Leu side chains) and charged aminoacid (L-Orn). It exhibits strong antibiotic activity towards ] and ] and even several pathogenic fungi.<ref name="pmid8810288">{{cite journal | vauthors = Kondejewski LH, Farmer SW, Wishart DS, Kay CM, Hancock RE, Hodges RS|author3-link=David S. Wishart | s2cid = 2015112 | title = Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs | journal = The Journal of Biological Chemistry | volume = 271 | issue = 41 | pages = 25261–8 | date = October 1996 | pmid = 8810288 | doi = 10.1074/jbc.271.41.25261 | doi-access = free }}</ref> The mode of action is not entirely agreed upon, but it is generally accepted that it is disruption of the lipid membrane and enhancement of the permeability of the bacterial cytoplasmic membrane.<ref name="pmid9201936">{{cite journal | vauthors = Prenner EJ, Lewis RN, Neuman KC, Gruner SM, Kondejewski LH, Hodges RS, McElhaney RN | title = Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity | journal = Biochemistry | volume = 36 | issue = 25 | pages = 7906–16 | date = June 1997 | pmid = 9201936 | doi = 10.1021/bi962785k }}</ref> Unfortunately, being ] at even low concentrations, gramicidin S is only used as topical applications at present. Additionally, Gramicidin S has been employed as a spermicide and therapeutic for genital ulcers caused by ].<ref>{{cite book | vauthors = Krylov YF | date = 1993 | title = Compendium of Medicinal Products of Russia | publisher = Inpharmchem Press | location = Moscow | pages = 343 | language = Russian }}</ref>
{{clear}}

⚫ == References ==
{{Reflist}}

{{Membrane proteins}}

⚫ ]
]
]
]

Latest revision as of 06:32, 5 January 2024

Chemical compound

Pharmaceutical compound
Gramicidin S
Structural formula of Gramicidin S
Ball-and-stick model of the Gramicidin S molecule
Clinical data
Routes of
administration		Topical
Identifiers
IUPAC name
  • Gramicidin S
CAS Number
PubChem CID
ChemSpider
UNII
ChEBI
ChEMBL
NIAID ChemDB
CompTox Dashboard (EPA)
Chemical and physical data
FormulaC60H92N12O10
Molar mass1141.470 g·mol
3D model (JSmol)
SMILES
  • CC(C)C1C(=O)N(C(=O)N2CCC2C(=O)N(C(=O)N(C(=O)N(C(=O)N(C(=O)N3CCC3C(=O)N(C(=O)N(C(=O)N1)CCCN)C(C)C)Cc4ccccc4)CC(C)C)CCCN)C(C)C)Cc5ccccc5
InChI
  • InChI=1S/C60H92N12O10/c1-35(2)31-43-53(75)67-45(33-39-19-11-9-12-20-39)59(81)71-29-17-25-47(71)55(77)70-50(38(7)8)58(80)64-42(24-16-28-62)52(74)66-44(32-36(3)4)54(76)68-46(34-40-21-13-10-14-22-40)60(82)72-30-18-26-48(72)56(78)69-49(37(5)6)57(79)63-41(23-15-27-61)51(73)65-43/h9-14,19-22,35-38,41-50H,15-18,23-34,61-62H2,1-8H3,(H,63,79)(H,64,80)(H,65,73)(H,66,74)(H,67,75)(H,68,76)(H,69,78)(H,70,77)/t41-,42-,43-,44-,45+,46+,47-,48-,49-,50-/m0/s1
  • Key:IUAYMJGZBVDSGL-XNNAEKOYSA-N
  (verify)

Gramicidin S or Gramicidin Soviet is an antibiotic that is effective against some gram-positive and gram-negative bacteria as well as some fungi.

It is a derivative of gramicidin, produced by the gram-positive bacterium Brevibacillus brevis. Gramicidin S is a cyclodecapeptide, constructed as two identical pentapeptides joined head to tail, formally written as cyclo(-Val-Orn-Leu-D-Phe-Pro-)2. That is to say, it forms a ring structure composed of five different amino acids, each one used twice within the structure. Another interesting point is that it utilizes two amino acids uncommon in peptides: ornithine as well as the atypical stereoisomer of phenylalanine. It is synthesized by gramicidin S synthetase.

Biosynthesis

Gramicidin S biosynthetic pathway consists of two-enzyme of nonribosomal peptide synthases (NRPSs), gramicidin S synthetase I (GrsA) and gramicidin S synthetase II (GrsB), to give a product as a cyclic decapeptide. Within the biosynthetic pathway, there are total of five modules that specifically recognize, activate, and condense the amino acids to gramicidin S. Starting module GrsA consists of three domains: Adenylation (A) domain where it incorporates the amino acid and activates it by adenylation using ATP, Thiolation (T) domain or peptidyl carrier protein (PCP) in which the adenylated amino acid gets covalently attached to the 4´-phosphopantetheine group and this gets loaded onto the conserved serine in the T domain, Epimerization (E) domain where it epimerizes L-amino acid to D-amino acid. Starting module GrsA loads D-Phe onto the system.

Second enzyme cluster GrsB contains four modules, each containing condensation (C), adenylation (A), and thiolation (T) domains and thioesterase domain (TE) at the end. C domain forms a peptide bond between two amino acids, D-Phe and L-Pro. L-Val, L-Orn, and L-Leu are incorporated sequentially by the next three modules of GrsB. After repeating the whole module synthesis once again, TE domain cyclizes and releases the two peptides and dimerize them together to form the final product.

Biosynthetic pathway of gramicidin S

History

Gramicidin S was discovered by Russian microbiologist Georgyi Frantsevitch Gause and his wife Maria Brazhnikova in 1942. Within the year Gramicidin S was being used in Soviet military hospitals to treat infection and eventually found usage at the front lines of combat by 1946. Gause was awarded the Stalin Prize for Medicine for his discovery in 1946. In 1944, Gramicidin S was sent by the Ministry of Health of the USSR to Great Britain via the International Red Cross in a collaborative effort to establish the exact structure. English chemist Richard Synge proved that the compound was an original antibiotic and a polypeptide using paper chromatography. He would later go on to receive the Nobel Prize for his work in chromatography. The crystal structure was finally established by Dorothy Hodgkin and Gerhard Schmidt; Margaret Thatcher worked for a term in 1947 with Gerhard Schmidt on the antibiotic Gramicidin S, as an undergraduate research project. The importance of Gramicidin S and antibiotic research in general was so great that Gause was not persecuted during the period of Lysenkoism in the USSR, while many of his colleagues were. Indeed, it was his need for developing new strains to mass-produce antibiotics that allowed politically sanctioned collaborations with geneticists like Joseph Rapoport and Alexander Malinovsky, who would both actively participate in the downfall of Lysenkoism.

Structure and pharmacological effect

Crystal structure of modified Gramicidin S. Modification includes Boc groups on the ornithine as well as methylation of select amide nitrogens to force cyclic conformation.

Gramicidin S differs from other gramicidin types in that it is a cationic cyclic decapeptide and has a structure of an anti-parallel beta-sheet. Gramicidin S molecule is amphiphilic, with hydrophobic amino acids (D-Phe, Val, Leu side chains) and charged aminoacid (L-Orn). It exhibits strong antibiotic activity towards Gram-negative and Gram-positive and even several pathogenic fungi. The mode of action is not entirely agreed upon, but it is generally accepted that it is disruption of the lipid membrane and enhancement of the permeability of the bacterial cytoplasmic membrane. Unfortunately, being hemolytic at even low concentrations, gramicidin S is only used as topical applications at present. Additionally, Gramicidin S has been employed as a spermicide and therapeutic for genital ulcers caused by sexually transmitted disease.

References

  1. Gause GF, Brazhnikova MG (1944). "Gramicidin S and its use in the Treatment of Infected Wounds". Nature. 154 (3918): 703. Bibcode:1944Natur.154..703G. doi:10.1038/154703a0. S2CID 4125407.
  2. Llamas-Saiz AL, Grotenbreg GM, Overhand M, van Raaij MJ (March 2007). "Double-stranded helical twisted beta-sheet channels in crystals of gramicidin S grown in the presence of trifluoroacetic and hydrochloric acids". Acta Crystallographica. Section D, Biological Crystallography. 63 (Pt 3): 401–7. Bibcode:2007AcCrD..63..401L. doi:10.1107/S0907444906056435. PMID 17327677.
  3. Conti E, Stachelhaus T, Marahiel MA, Brick P (July 1997). "Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S". The EMBO Journal. 16 (14): 4174–83. doi:10.1093/emboj/16.14.4174. PMC 1170043. PMID 9250661.
  4. Stachelhaus T, Marahiel MA (March 1995). "Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA". The Journal of Biological Chemistry. 270 (11): 6163–9. doi:10.1074/jbc.270.11.6163. PMID 7534306. S2CID 10325408.
  5. von Döhren H, Keller U, Vater J, Zocher R (November 1997). "Multifunctional Peptide Synthetases". Chemical Reviews. 97 (7): 2675–2706. doi:10.1021/cr9600262. PMID 11851477.
  6. Sieber SA, Marahiel MA (February 2005). "Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics". Chemical Reviews. 105 (2): 715–38. doi:10.1021/cr0301191. PMID 15700962.
  7. Miller LM, Mazur MT, McLoughlin SM, Kelleher NL (October 2005). "Parallel interrogation of covalent intermediates in the biosynthesis of gramicidin S using high-resolution mass spectrometry". Protein Science. 14 (10): 2702–12. doi:10.1110/ps.051553705. PMC 2253301. PMID 16195555.
  8. ^ Gall YM, Konashev MB (2001). "The discovery of Gramicidin S: the intellectual transformation of G.F. Gause from biologist to researcher of antibiotics and on its meaning for the fate of Russian genetics". History and Philosophy of the Life Sciences. 23 (1): 137–50. PMID 12212443.
  9. "R.L.M. Synge (British biochemist)". Britannica Online Encyclopedia. 24 October 2023.
  10. Yamada K, Unno M, Kobayashi K, Oku H, Yamamura H, Araki S, et al. (October 2002). "Stereochemistry of protected ornithine side chains of gramicidin S derivatives: X-ray crystal structure of the bis-Boc-tetra-N-methyl derivative of gramicidin S". Journal of the American Chemical Society. 124 (43): 12684–8. doi:10.1021/ja020307t. PMID 12392415.
  11. Kondejewski LH, Farmer SW, Wishart DS, Kay CM, Hancock RE, Hodges RS (October 1996). "Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs". The Journal of Biological Chemistry. 271 (41): 25261–8. doi:10.1074/jbc.271.41.25261. PMID 8810288. S2CID 2015112.
  12. Prenner EJ, Lewis RN, Neuman KC, Gruner SM, Kondejewski LH, Hodges RS, McElhaney RN (June 1997). "Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity". Biochemistry. 36 (25): 7906–16. doi:10.1021/bi962785k. PMID 9201936.
  13. Krylov YF (1993). Compendium of Medicinal Products of Russia (in Russian). Moscow: Inpharmchem Press. p. 343.
Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)
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Membrane-spanning 4A
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Pulmonary surfactant
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