Volume : 13, Issue : 08, August – 2026
Title:
FROM PEPTIDES TO PEPTIDOMIMETICS: CHEMICAL AND STRUCTURAL STRATEGIES FOR DEVELOPING DRUG-LIKE THERAPEUTICS: A STRATEGY-FOCUSED NARRATIVE REVIEW FOR MEDICINAL CHEMISTRY AND DRUG DISCOVERY
Authors :
Omkar Rai*, Soma Sekhar Pulamarasetti, Manish Gupta, Shibu Kumar, Varri Anudeepthi
Abstract :
Peptides have important properties in between small molecules and biologics; they are able to bind broadly and with high affinity and selectivity to protein surfaces that are shallow, dynamic and rich in conformational and nonpolar interactions, but are often hindered for clinical translation by factors such as proteolysis, conformational flexibility, lack of membrane permeability, rapid clearance and low oral exposure. Peptidomimetics solve these disadvantages by preserving the spatial geometry of essential recognition components while substituting some of the peptide’s components with noncanonical residues, backbone modifications, bioisosteres, conformational constraints, and/or physicochemical-property modifiers. The present review offers a strategy-oriented framework for the development of a bioactive peptide to a drug-like peptidomimetic. The following six interconnected design classes are explored: (i) incorporation of unnatural and noncanonical amino-acids, (ii) backbone engineering and peptide-bond replacement, (iii) terminal and side-chain modification, (iv) cyclization and macrocyclization, (v) stapling and other conformational-locking strategies, and (vi) integrated molecular optimization of affinity, selectivity, stability, permeability, and pharmacokinetics. Special attention is given to structure–activity relationships, targeting of protein–protein interactions, oral delivery, intracellular delivery and optimization using computation. Examples of antiviral, anticancer, antimicrobial and enzyme-inhibitor and receptor-directed drug discovery demonstrate how single changes can address individual liabilities, but can also result in trade-offs. A practical design workflow is proposed that sees structural information, medicinal-chemistry iteration, biophysical characterization, permeability/stability assays and pharmacokinetic profiling are not optimized independently but rather integrated. It is concluded that successful peptidomimetic design is not about maximising any single property, but about an appropriate combination of recognition geometry and physicochemical and pharmacokinetic properties.
Keywords: Peptidomimetics; peptide drug discovery; unnatural amino acids; noncanonical amino acids; backbone engineering; macrocyclization; stapled peptides; conformational restriction; protein–protein interactions; medicinal chemistry; drug-like peptides.
Cite This Article:
Please cite this article in press Omkar Rai et al., From Peptides To Peptidomimetics: Chemical And Structural Strategies For Developing Drug-Like Therapeutics: A Strategy-Focused Narrative Review For Medicinal Chemistry And Drug Discovery. Indo Am. J. P. Sci, 2026; 13(08).
REFERENCES:
1. Muttenthaler M, King GF, Adams DJ, Alewood PF. Trends in peptide drug discovery. Nat Rev Drug Discov. 2021. DOI: 10.1038/s41573-020-00135-8
2. Craik DJ, Fairlie DP, Liras S, Price D. The future of peptide-based drugs. Chem Biol Drug Des. 2013. DOI: 10.1111/cbdd.12055
3. Lau JL, Dunn MK. Therapeutic peptides: historical perspectives, current development trends, and future directions. Bioorg Med Chem. 2018. DOI: 10.1016/j.bmc.2017.06.052
4. Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M. Synthetic therapeutic peptides: science and market. Drug Discov Today. 2010. DOI: 10.1016/j.drudis.2009.10.009
5. Tsomaia N. Peptide therapeutics: targeting the undruggable space. Eur J Med Chem. 2015. DOI: 10.1016/j.ejmech.2015.01.014
6. Adessi C, Soto C. Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr Med Chem. 2002. DOI: 10.2174/0929867023372862
7. Gentilucci L, De Marco R, Cerisoli L. Chemical modifications designed to improve peptide stability: incorporation of non-natural amino acids, pseudo-peptide bonds, and cyclization. Curr Pharm Des. 2010. DOI: 10.2174/138161210791293194
8. Avan I, Hall CD, Katritzky AR. Peptidomimetics via modifications of amino acids and peptide bonds. Chem Soc Rev. 2014. DOI: 10.1039/C3CS60384A
9. Lenci E, Trabocchi A. Peptidomimetic toolbox for drug discovery. Chem Soc Rev. 2020. DOI: 10.1039/D0CS00102C
10. Qvit N, Rubin SJS, Urban TJ, Mochly-Rosen D, Gross ER. Peptidomimetic therapeutics: scientific approaches and opportunities. Drug Discov Today. 2017. DOI: 10.1016/j.drudis.2016.11.003
11. Perez JJ. Designing Peptidomimetics. Curr Top Med Chem. 2018. DOI: 10.2174/1568026618666180522075258
12. Li Petri G, Di Martino S, De Rosa M. Peptidomimetics: An Overview of Recent Medicinal Chemistry Efforts toward the Discovery of Novel Small Molecule Inhibitors. J Med Chem. 2022. DOI: 10.1021/acs.jmedchem.2c00123
13. Zhang G, Andersen J, Gerona-Navarro G. Peptidomimetics Targeting Protein-Protein Interactions for Therapeutic Development. Protein Pept Lett. 2018. DOI: 10.2174/0929866525666181101100842
14. Cunningham AD, Qvit N, Mochly-Rosen D. Peptides and peptidomimetics as regulators of protein-protein interactions. Curr Opin Struct Biol. 2017. DOI: 10.1016/j.sbi.2016.12.009
15. Corbi-Verge C, Garton M, Nim S, Kim PM. Strategies to Develop Inhibitors of Motif-Mediated Protein-Protein Interactions as Drug Leads. Annu Rev Pharmacol Toxicol. 2017. DOI: 10.1146/annurev-pharmtox-010716-104805
16. Mabonga L, Kappo AP. Peptidomimetics: A Synthetic Tool for Inhibiting Protein–Protein Interactions in Cancer. Int J Pept Res Ther. 2020. DOI: 10.1007/s10989-019-09831-5
17. Watkins AM, Bonneau R, Arora PS. Modeling and Design of Peptidomimetics to Modulate Protein-Protein Interactions. Methods Mol Biol. 2017. DOI: 10.1007/978-1-4939-6798-8_17
18. Mizuno A, Matsui K, Shuto S. From Peptides to Peptidomimetics: A Strategy Based on the Structural Features of Cyclopropane. Chemistry. 2017. DOI: 10.1002/chem.201702119
19. Doti N, Mardirossian M, Sandomenico A, Ruvo M, Caporale A. Recent Applications of Retro-Inverso Peptides. Int J Mol Sci. 2021. DOI: 10.3390/ijms22168677
20. Fletcher MD, Campbell MM. Partially Modified Retro-Inverso Peptides: Development, Synthesis, and Conformational Behavior. Chem Rev. 1998. DOI: 10.1021/cr970468t
21. Preston GW. Different directions for retro-inverso peptides. J Pept Sci. 2022. DOI: 10.1002/psc.3384
22. Al Musaimi O. Unlocking the Potential of Retro-Inverso (RI) Peptides as Future Drug Candidates. Int J Pept Res Ther. 2024. DOI: 10.1007/s10989-024-10639-1
23. Rezhdo A, Islam M, Huang M, Van Deventer JA. Future prospects for noncanonical amino acids in biological therapeutics. Curr Opin Biotechnol. 2019. DOI: 10.1016/j.copbio.2019.02.020
24. Hickey JL, Sindhikara D, Zultanski SL, et al. Beyond 20 in the 21st Century: Prospects and Challenges of Non-canonical Amino Acids in Peptide Drug Discovery. ACS Med Chem Lett. 2023. DOI: 10.1021/acsmedchemlett.3c00037
25. Unnatural Amino Acids: Strategies, Designs, and Applications in Medicinal Chemistry and Drug Discovery. Unnatural Amino Acids: Strategies, Designs, and Applications in Medicinal Chemistry and Drug Discovery. J Med Chem. 2024. DOI: 10.1021/acs.jmedchem.4c00110
26. Borchardt RT, Aubé J, Siahaan TJ, Gangwar S, Pauletti GM. Improvement of oral peptide bioavailability: Peptidomimetics and prodrug strategies. Adv Drug Deliv Rev. 1997. DOI: 10.1016/S0169-409X(97)00045-8
27. Samanen J, Wilson G, Smith PL, et al. Chemical approaches to improve the oral bioavailability of peptidergic molecules. J Pharm Pharmacol. 1996. DOI: 10.1111/j.2042-7158.1996.tb07111.x
28. Biron E, Chatterjee J, Ovadia O, et al. Improving oral bioavailability of peptides by multiple N-methylation: somatostatin analogues. Angew Chem Int Ed. 2008. DOI: 10.1002/anie.200703295
29. Passioura T, Katoh T, Goto Y, Suga H. Selection-based discovery of druglike macrocyclic peptides. Annu Rev Biochem. 2014. DOI: 10.1146/annurev-biochem-060713-035456
30. Vinogradov AA, Yin Y, Suga H. Macrocyclic Peptides as Drug Candidates: Recent Progress and Remaining Challenges. J Am Chem Soc. 2019. DOI: 10.1021/jacs.8b13178
31. Bechtler C, Lamers C. Macrocyclization strategies for cyclic peptides and peptidomimetics. RSC Med Chem. 2021. DOI: 10.1039/D1MD00083G
32. Pei D. Understanding Cell Penetration of Cyclic Peptides. Chem Rev. 2019. DOI: 10.1021/acs.chemrev.9b00008
33. Lau YH, de Andrade P, Wu Y, Spring DR. Peptide stapling techniques based on different macrocyclisation chemistries. Chem Soc Rev. 2015. DOI: 10.1039/C4CS00246F
34. Walensky LD, Bird GH. Hydrocarbon-stapled peptides: principles, practice, and progress. J Med Chem. 2014. DOI: 10.1021/jm4011675
35. Ali AM, Atmaj J, Van Oosterwijk N, Groves MR, Dömling A. Stapled Peptides Inhibitors: A New Window for Target Drug Discovery. Comput Struct Biotechnol J. 2019. DOI: 10.1016/j.csbj.2019.01.012
36. Xie X, Gao L, Shull AY, Teng Y. Stapled peptides: providing the best of both worlds in drug development. Future Med Chem. 2016. DOI: 10.4155/fmc-2016-0102
37. Fairlie DP, Dantas de Araujo A. Review stapling peptides using cysteine crosslinking. Biopolymers. 2016. DOI: 10.1002/bip.22877
38. Kneissl S, Loveridge EJ, Williams C, Crump MP, Allemann RK. Photocontrollable peptide-based switches target the anti-apoptotic protein Bcl-xL. ChemBioChem. 2008. DOI: 10.1002/cbic.200800502
39. Chang YS, Graves B, Guerlavais V, et al. Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy. Proc Natl Acad Sci USA. 2013. DOI: 10.1073/pnas.1303002110
40. Felix AM, Heimer EP, Wang CT, et al. Synthesis, biological activity and conformational analysis of cyclic GRF analogs. Int J Pept Protein Res. 1988. DOI: 10.1111/j.1399-3011.1988.tb01375.x
41. Greenfield N, Fasman GD. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 1969. DOI: 10.1021/bi00838a031
42. Shepherd NE, Hoang HN, Abbenante G, Fairlie DP. Single turn peptide alpha helices with exceptional stability in water. J Am Chem Soc. 2005. DOI: 10.1021/ja0456003
43. Khoo KK, Wilson MJ, Smith BJ, et al. Lactam-stabilized helical analogues of the analgesic μ-conotoxin KIIIA. J Med Chem. 2011. DOI: 10.1021/jm200839a
44. Moses JE, Moorhouse AD, Kolb HC, Finn MG, Sharpless KB. The growing applications of click chemistry. Chem Soc Rev. 2007. DOI: 10.1039/B613014N
45. Kawamoto SA, Coleska A, Ran X, et al. Design of triazole-stapled BCL9 α-helical peptides to target the β-catenin/BCL9 protein-protein interaction. J Med Chem. 2012. DOI: 10.1021/jm201125d
46. Madden MM, Muppidi A, Li Z, et al. Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition. Bioorg Med Chem Lett. 2011. DOI: 10.1016/j.bmcl.2011.01.004
47. Haney CM, Loch MT, Horne WS. Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links. Chem Commun. 2011. DOI: 10.1039/C1CC12010G
48. Spokoyny AM, Zou Y, Ling JJ, et al. A Perfluoroaryl-cysteine SNAr chemistry approach to unprotected peptide stapling. J Am Chem Soc. 2013. DOI: 10.1021/ja400119t
49. Brunel FM, Dawson PE. Synthesis of constrained helical peptides by thioether ligation: application to analogs of gp41. Chem Commun. 2005. DOI: 10.1039/B419015G
50. Briggs LC, Chan AWE, Davis CA, et al. IKKγ-mimetic peptides block the resistance to apoptosis associated with Kaposi’s sarcoma-associated herpesvirus infection. J Virol. 2017. DOI: 10.1128/JVI.01170-17
51. Rennie YK, McIntyre PJ, Akindele T, et al. A TPX2 Proteomimetic has enhanced affinity for Aurora-A due to hydrocarbon stapling of a helix. ACS Chem Biol. 2016. DOI: 10.1021/acschembio.6b00727
52. Phillips NB, Wan ZL, Whittaker L, et al. Supramolecular protein engineering: design of zinc-stapled insulin hexamers as a long acting depot. J Biol Chem. 2010. DOI: 10.1074/jbc.C110.105825
53. Xu W, Lau YH, Fischer G, et al. Macrocyclized extended peptides: inhibiting the substrate-recognition domain of Tankyrase. J Am Chem Soc. 2017. DOI: 10.1021/jacs.6b10234
54. Gunzburg MJ, Kulkarni K, Watson GM, et al. Unexpected involvement of staple leads to redesign of selective bicyclic peptide inhibitor of Grb7. Sci Rep. 2016. DOI: 10.1038/srep27060
55. Ultsch M, Braisted A, Maun HR, Eigenbrot C. 3-2-1: structural insights from stepwise shrinkage of a three-helix Fc-binding domain to a single helix. Protein Eng Des Sel. 2017. DOI: 10.1093/protein/gzx029
56. Lama D, Quah ST, Verma CS, et al. Rational optimization of conformational effects induced by hydrocarbon staples in peptides and their binding interfaces. Sci Rep. 2013. DOI: 10.1038/srep03451
57. McGrath S, Tortorici M, Drouin L, et al. Structure-enabled discovery of a stapled peptide inhibitor to target the oncogenic transcriptional repressor TLE1. Chem Eur J. 2017. DOI: 10.1002/chem.201700747
58. Kussie PH, Gorina S, Marechal V, et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science. 1996. DOI: 10.1126/science.274.5289.948
59. Baek S, Kutchukian PS, Verdine GL, et al. Structure of the stapled p53 peptide bound to Mdm2. J Am Chem Soc. 2012. DOI: 10.1021/ja2090367
60. Chee SMQ, Wongsantichon J, Soo Tng Q, et al. Structure of a stapled peptide antagonist bound to nutlin-resistant Mdm2. PLoS One. 2014. DOI: 10.1371/journal.pone.0104914
61. Lau YH, Wu Y, Rossmann M, et al. Double strain-promoted macrocyclization for the rapid selection of cell-active stapled peptides. Angew Chem Int Ed. 2015. DOI: 10.1002/anie.201508416
62. Chee SMQ, Wongsantichon J, Siau J, et al. Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids. PLoS One. 2017. DOI: 10.1371/journal.pone.0189379
63. Stewart ML, Fire E, Keating AE, Walensky LD. The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer. Nat Chem Biol. 2010. DOI: 10.1038/nchembio.391
64. Miles JA, Yeo DJ, Rowell P, et al. Hydrocarbon constrained peptides-understanding preorganisation and binding affinity. Chem Sci. 2016. DOI: 10.1039/C5SC04048E
65. Rezaei Araghi R, Bird GH, Ryan JA, et al. Iterative optimization yields MCL-1-targeting stapled peptides with selective cytotoxicity to MCL-1-dependent cancer cells. Proc Natl Acad Sci USA. 2018. DOI: 10.1073/pnas.1712952115
66. Harvey EP, Seo HS, Guerra RM, et al. Crystal structures of anti-apoptotic BFL-1 and its complex with a covalent stapled peptide inhibitor. Structure. 2018. DOI: 10.1016/j.str.2017.11.016
67. Phillips C, Roberts LR, Schade M, et al. Design and structure of stapled peptides binding to estrogen receptors. J Am Chem Soc. 2011. DOI: 10.1021/ja202946k
68. Speltz TE, Fanning SW, Mayne CG, et al. Stapled peptides with γ-methylated hydrocarbon chains for the estrogen receptor/coactivator interaction. Angew Chem Int Ed. 2016. DOI: 10.1002/anie.201510557
69. Speltz TE, Mayne CG, Fanning SW, et al. A “cross-stitched” peptide with improved helicity and proteolytic stability. Org Biomol Chem. 2018. DOI: 10.1039/C8OB00790J
70. Frank AO, Vangamudi B, Feldkamp MD, et al. Discovery of a potent stapled helix peptide that binds to the 70N domain of replication protein A. J Med Chem. 2014. DOI: 10.1021/jm401730y
71. Grossmann TN, Yeh JTH, Bowman BR, et al. Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin. Proc Natl Acad Sci USA. 2012. DOI: 10.1073/pnas.1208396109
72. Findeisen F, Campiglio M, Jo H, et al. Stapled voltage-gated calcium channel α-interaction domain peptides act as selective protein-protein interaction inhibitors. ACS Chem Neurosci. 2017. DOI: 10.1021/acschemneuro.6b00454
73. Lee Y, Yoon H, Hwang SM, et al. Targeted inhibition of the NCOA1/STAT6 protein-protein interaction. J Am Chem Soc. 2017. DOI: 10.1021/jacs.7b08972
74. Wu Y, Villa F, Maman J, et al. Targeting the genome-stability hub Ctf4 by stapled-peptide design. Angew Chem Int Ed. 2017. DOI: 10.1002/anie.201705611
75. Haney CM, Horne WS. Oxime side-chain cross-links in an α-helical coiled-coil protein: structure, thermodynamics, and folding-templated synthesis of bicyclic species. Chem Eur J. 2013. DOI: 10.1002/chem.201300506
76. Tan WL, Wong KH, Lei J, et al. Lybatides from Lycium barbarum contain an unusual cystine-stapled helical peptide scaffold. Sci Rep. 2017. DOI: 10.1038/s41598-017-05037-1
77. Jaskolski M, Wlodawer A, Tomasselli AG, et al. Structure at 2.5-Å resolution of chemically synthesized HIV-1 protease complexed with a hydroxyethylene-based inhibitor. Biochemistry. 1991. DOI: 10.1021/bi00220a023
78. Swain AL, Miller MM, Green J, et al. X-ray crystallographic structure of a complex between HIV-1 protease and a substrate-based hydroxyethylamine inhibitor. Proc Natl Acad Sci USA. 1990. DOI: 10.1073/pnas.87.22.8805
79. Bhattacharya S, Zhang H, Debnath AK, Cowburn D. Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid. J Biol Chem. 2008. DOI: 10.1074/jbc.C800048200
80. Singh PK, Solanki V, Sharma S, et al. The intramolecular disulfide-stapled structure of laterosporulin. FEBS J. 2015. DOI: 10.1111/febs.13129
81. Douse CH, Maas SJ, Thomas JC, et al. Crystal structures of stapled and hydrogen bond surrogate peptides targeting a fully buried protein-helix interaction. ACS Chem Biol. 2014. DOI: 10.1021/cb500271c
82. Byrne C, McEwan PA, Emsley J, et al. End-stapled homo and hetero collagen triple helices: a click chemistry approach. Chem Commun. 2011. DOI: 10.1039/C0CC04795C
83. Mercurio FA, Pirone L, Di Natale C, et al. SAM domain-based stapled peptides: structural analysis and interaction studies. Bioorg Chem. 2018. DOI: 10.1016/j.bioorg.2018.07.013
84. De Paola I, Pirone L, Palmieri M, et al. Cullin3-BTB interface: a novel target for stapled peptides. PLoS One. 2015. DOI: 10.1371/journal.pone.0121149
85. Barthe P, Roumestand C, Rochette S, Vita C. Synthesis and NMR solution structure of an α-helical hairpin stapled with two disulfide bridges. Protein Sci. 2000. DOI: 10.1110/ps.9.5.942
86. Fear G, Komarnytsky S, Raskin I. Protease inhibitors and their peptidomimetic derivatives as potential drugs. Pharmacol Ther. 2007. DOI: 10.1016/j.pharmthera.2006.09.001
87. Ding D, Xu S, da Silva-Júnior EF, Liu X, Zhan P. Medicinal chemistry insights into antiviral peptidomimetics. Drug Discov Today. 2023. DOI: 10.1016/j.drudis.2022.103468
88. Molchanova N, Hansen PR, Franzyk H. Advances in Development of Antimicrobial Peptidomimetics as Potential Drugs. Molecules. 2017. DOI: 10.3390/molecules22091430
89. Méndez-Samperio P. Peptidomimetics as a new generation of antimicrobial agents: current progress. Infect Drug Resist. 2014. DOI: 10.2147/IDR.S49229
90. Hellewell L, Malek Gilani N, Stanton CJ, et al. Efficacy of natural antimicrobial peptides versus peptidomimetic analogues: a systematic review. Future Med Chem. 2022. DOI: 10.4155/fmc-2022-0160
Volume : 13, Issue : 08, August – 2026
Title:
EVALUATION OF ANTIHYPERLIPIDEMIC ACTIVITY OF SAPINDUS EMARGINATUS IN RATS
Authors :
Chinthala Jamima*, Dr.R.narasimha Rao, Dr.N. Raghunandhan
Abstract :
Obesity and hyperlipidemia have become major disorders predominantly causing prevailing cardiovascular diseases and ultimately death. The prolonged use of anti-obesity drugs and statins for reducing obesity and blood lipid levels is leading toward adverse effects of kidneys and muscles, specifically rhabdomyolysis. The objective of this study is to evaluate potential of seeds of Sapindus emarginatus against hyperlipidemia. In this model of Hyperlipidemia, 30 adult male wistar rats (200-250gms) were evenly divided into 5 groups in both groups. Group-1 and Group-2 served as untreated and model controls respectively, while Group-3, 4 and 5 were the treatments groups which were simultaneously treated with standard, 100 and 200 mg/kg extract respectively along with High Fat Diet. On last day, blood samples for biochemical parameters, were obtained under inhaled diether anaesthesia. The outcomes of this study were expressed as mean standard error and data were evaluated by using analysis of variance followed by multiple comparisons. Oral administration of 100 mg/ kg and 200mg/kg body weight of Methanolic extract residual fraction of Moringa oleifera. Leaves exhibited a significant reduction (P < 0.01) in serum lipid parameters such as triglycerides, total cholesterol, low density lipoprotein (LDL), very LDL and increase in high density lipoprotein in hyperlipidemic rats when compared with hyperlipidemic control in both models. Our results demonstrated that Methanolic extract fraction of Sesbania grandiflora. Possessed significant antihyperlipidemic activity.
Keywords: Sesbania grandiflora, Cholesterol, LDL, triglycerides and antihyperlipidemic activity.
Cite This Article:
Please cite this article in press Chinthala Jamimaet al., Evaluation of Antihyperlipidemic activity of Sapindus Emarginatus in rats,, Indo Am. J. P. Sci, 2026; 13(08).
REFERENCES:
1. Amit G, Vandana S, Sidharth M. HYPERLIPIDEMIA: An Updated Review. Inter J of Biopharma & Toxicol Res 2011;1:81-89.
2. Virchow RP, Thrombose IG. In Gesammelte Abhandlungen zur Wissenschaftlichen Medicin. Frankfurt-am-Main, Meidinger Sohn & Company 1856, S 458-564.
3. Ankur rohilla, Nidhi Dagar, Seema Rohilla, Amarjeet Dahiya, Ashok Kushnoor. HYPERLIPIDEMIA- a deadly pathological condition. Inter J Curr Pharma Res 2012;4:15-18
4. Ross R, Glomset JA. The pathogenesis of atherosclerosis. N Engl J Med 1976;295:369-77.
5. Grundy SM, Vega GL. Hypertriglyceridemia: causes and relation to coronary heart disease – Semin. Thromb. Hemost 1988;14:249-64.
6. Dargel R. Lipoproteins and the etiopathogenesis of atherosclerosis. Zentralbl Allg Pathol 1989; 135: 501-504.




