LL-37(human)
目录号 : GC25579LL-37, human is a 37-residue, amphipathic, cathelicidin-derived peptide, which exhibits a broad spectrum of antimicrobial activity.
Cas No.:597562-32-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
LL-37, human is a 37-residue, amphipathic, cathelicidin-derived peptide, which exhibits a broad spectrum of antimicrobial activity.
[1] DÜrr UH, et al. Biochim Biophys Acta. 2006 Sep;1758(9):1408-25.
| Cas No. | 597562-32-8 | SDF | Download SDF |
| 分子式 | C205H341N61O52 | 分子量 | 4492.28 |
| 溶解度 | DMSO: Insoluble;Water: 90 mg/mL (20.03 mM);Ethanol: 90 mg/mL (20.03 mM) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.2226 mL | 1.113 mL | 2.226 mL |
| 5 mM | 0.0445 mL | 0.2226 mL | 0.4452 mL |
| 10 mM | 0.0223 mL | 0.1113 mL | 0.2226 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Interaction of LL-37 human cathelicidin peptide with a model microbial-like lipid membrane
Bioelectrochemistry 2021 Oct;141:107842.PMID:34049238DOI:10.1016/j.bioelechem.2021.107842.
The only representative of cathelicidin peptides in humans is LL-37, a multifunctional antimicrobial peptide (AMP) that is a part of the innate immune response. Details of the LL-37 direct activity against pathogens are not well understood at the molecular level. Here, we present research on the mechanism of interaction between LL-37 and a model multicomponent bilayer lipid membrane (BLM), mimicking microbial cell membrane. Electrochemical impedance spectroscopy (EIS), high-resolution atomic force microscopy (AFM) imaging, and polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS) were applied to study the peptide influence on a model microbial-like membrane. We show that LL-37 causes changes in the phospholipid molecules conformation and orientation, leading to membrane disintegration, significantly affecting the membrane electrical parameters, such as capacitance and resistance. High-resolution AFM imaging shows topographical and mechanical effects of such disintegration, while PM-IRRAS data indicates that introduction of LL-37 causes changes in the phospholipid acyl chains from all-trans to gauche conformations. Moreover, the presence of LL-37 significantly alters the value of the phospholipid tilt angle. Altogether, our results suggest a "carpet" membrane dissolution followed by a detergent-like membrane disruption mechanism upon LL-37 activity. This research gives a novel insight into the understanding of LL-37 influence on multicomponent model membranes and a promising contribution to the development of LL-37-derived therapeutic agents against drug-resistant bacteria.
Role of Antimicrobial Peptides in Skin Barrier Repair in Individuals with Atopic Dermatitis
Int J Mol Sci 2020 Oct 14;21(20):7607.PMID:33066696DOI:10.3390/ijms21207607.
Atopic dermatitis (AD) is a common chronic inflammatory skin disease that exhibits a complex interplay of skin barrier disruption and immune dysregulation. Patients with AD are susceptible to cutaneous infections that may progress to complications, including staphylococcal septicemia. Although most studies have focused on filaggrin mutations, the physical barrier and antimicrobial barrier also play critical roles in the pathogenesis of AD. Within the physical barrier, the stratum corneum and tight junctions play the most important roles. The tight junction barrier is involved in the pathogenesis of AD, as structural and functional defects in tight junctions not only disrupt the physical barrier but also contribute to immunological impairments. Furthermore, antimicrobial peptides, such as LL-37, human b-defensins, and S100A7, improve tight junction barrier function. Recent studies elucidating the pathogenesis of AD have led to the development of barrier repair therapy for skin barrier defects in patients with this disease. This review analyzes the association between skin barrier disruption in patients with AD and antimicrobial peptides to determine the effect of these peptides on skin barrier repair and to consider employing antimicrobial peptides in barrier repair strategies as an additional approach for AD management.
SP-LL-37, human antimicrobial peptide, enhances disease resistance in transgenic rice
PLoS One 2017 Mar 10;12(3):e0172936.PMID:28282452DOI:10.1371/journal.pone.0172936.
human LL-37 is a multifunctional antimicrobial peptide of cathelicidin family. It has been shown in recent studies that it can serve as a host's defense against influenza A virus. We now demonstrate in this study how signal peptide LL-37 (SP-LL-37) can be used in rice resistance against bacterial leaf blight and blast. We synthesized LL-37 peptide and subcloned in a recombinant pPZP vector with pGD1 as promoter. SP-LL-37 was introduced into rice plants by Agrobacterium mediated transformation. Stable expression of SP-LL-37 in transgenic rice plants was confirmed by RT-PCR and ELISA analyses. Subcellular localization of SP-LL-37-GFP fusion protein showed evidently in intercellular space. Our data on testing for resistance to bacterial leaf blight and blast revealed that the transgenic lines are highly resistant compared to its wildtype. Our results suggest that LL-37 can be further explored to improve wide-spectrum resistance to biotic stress in rice.
LL-37 causes cell death of human nasal epithelial cells, which is inhibited with a synthetic glycosaminoglycan
PLoS One 2017 Aug 24;12(8):e0183542.PMID:28837619DOI:10.1371/journal.pone.0183542.
LL-37 is an immune peptide that regulates innate and adaptive immune responses in the upper airways. Elevated levels of LL-37 have been linked to cell death and inflammatory diseases, such as chronic rhinosinusitis (CRS). Glycosaminoglycans (GAGs) are polysaccharides that are found on respiratory epithelial cells and serve important roles in mucosal surface repair. Recent findings suggest that a synthetic glycosaminoglycan (GM-0111) can protect against LL-37-induced sinonasal mucosal inflammation and cell death in a murine model of acute RS. Herein, we elucidated the mechanisms by which LL-37 causes sinonasal inflammation and how GM-0111 can prevent these mechanisms. When challenged with LL-37, human nasal epithelial cells (HNEpCs) and mouse macrophages (J774.2) demonstrated increased release of adenosine triphosphate (ATP) and interleukin (IL)-6 and -8, as well as cell death and lysis. These cellular responses were all blocked dose-dependently by pre-treatment with GM-0111. We identified that LL-37-induced cell death is associated with caspase-1 and -8 activation, but not activation of caspase-3/7. These responses were again blocked by GM-0111. Our data suggest that LL-37 causes cellular death of HNEpCs and macrophages through the pro-inflammatory necrotic and/or pyroptotic pathways rather than apoptosis, and that a GM-0111 is capable of inhibiting these pro-inflammatory cellular events.
human antimicrobial peptides LL-37 and human β-defensin-2 reduce viral replication in keratinocytes infected with varicella zoster virus
Clin Exp Dermatol 2012 Jul;37(5):534-43.PMID:22639919DOI:10.1111/j.1365-2230.2012.04305.x.
Background: There is mounting evidence that antimicrobial peptides have an important role in cutaneous defence, but the expression of these antimicrobial peptides in atopic eczema (AE) is still unclear. There are several families of antimicrobial peptides, including cathelicidins and human β-defensins. Patients with AE are more susceptible to severe cutaneous viral infections, including varicella zoster virus (VZV). Aim: To characterize the functional activity of the antimicrobial peptides LL-37 (human cathelicidin) and human β-defensin (hBD)-2 keratinocytes were infected with VZV, in a skin-infection model. Methods: Flow-cytometry analysis was used to investigate LL-37 expression in normal human keratinocytes, and quantitative PCR was used to determine viral loads in infected HaCaT keratinocytes and B cells, with and without exogenous LL-37 and hBD-2. Results: LL-37 expression was present in keratinocytes, and both exogenous LL-37 and hBD-2 significantly reduced VZV load in infected keratinocytes and B cells. Specific antibodies blocked the antiviral action exhibited by these antimicrobial peptides. Pre-incubation of VZV with LL-37, but not hBD-2, further reduced VZV load. Conclusions: Both LL-37 and hBD-2 have an antiviral effect on VZV replication in the keratinocyte HaCaT cell line and in B cells, but their mechanism of action is different. Evidence of the relationship between antimicrobial peptide expression and higher susceptibility to infections in AE skin is still emerging. Developing novel antiviral therapies based on antimicrobial peptides may provide improved treatment options for patients with AE.